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ATP synthase subunit beta, mitochondrial (P00830)

Identification
NameATP synthase subunit beta, mitochondrial
SynonymsNot Available
Gene NameATP2
Enzyme Class
Biological Properties
General FunctionInvolved in ATP binding
Specific FunctionMitochondrial 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
Cellular LocationMitochondrion. Mitochondrion inner membrane.
SMPDB Pathways
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
purine nucleotides de novo biosynthesisPW002478 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Methane metabolismec00680 Map00680
Oxidative phosphorylationec00190 Map00190
SMPDB Reactions
ADP + phosphate + hydron ↔ water + hydron + Adenosine triphosphate
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
macromolecular complex
proton-transporting two-sector ATPase complex, catalytic domain
protein complex
proton-transporting two-sector ATPase complex
proton-transporting ATP synthase complex, catalytic core F(1)
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
catalytic activity
hydrogen-exporting ATPase activity, phosphorylative mechanism
nucleotide binding
pyrophosphatase activity
transporter activity
nucleoside-triphosphatase activity
transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
proton-transporting ATPase activity, rotational mechanism
hydrolase activity
monovalent inorganic cation transmembrane transporter activity
substrate-specific transmembrane transporter activity
hydrogen ion transmembrane transporter activity
ion transmembrane transporter activity
hydrogen ion transporting ATP synthase activity, rotational mechanism
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
binding
nucleoside binding
purine nucleoside binding
Process
proton transport
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
establishment of localization
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
transport
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
ATP synthesis coupled proton transport
purine nucleotide metabolic process
purine nucleoside triphosphate metabolic process
purine nucleotide biosynthetic process
purine ribonucleoside triphosphate metabolic process
purine nucleoside triphosphate biosynthetic process
ATP metabolic process
purine ribonucleoside triphosphate biosynthetic process
hydrogen transport
ATP biosynthetic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJR121W
Gene Sequence>1536 bp ATGGTTTTGCCAAGACTATATACTGCTACATCCCGTGCTGCTTTTAAAGCAGCCAAACAA TCCGCTCCGCTTCTATCCACTTCGTGGAAAAGATGTATGGCCTCAGCTGCTCAATCTACT CCAATCACCGGTAAAGTTACCGCTGTCATTGGTGCCATTGTTGACGTTCATTTTGAACAA TCAGAGTTGCCCGCTATTTTGAACGCTTTAGAAATTAAAACACCTCAAGGTAAGTTGGTT TTGGAAGTTGCTCAACATTTGGGTGAAAACACTGTCAGAACCATTGCTATGGATGGTACC GAAGGTTTGGTCCGTGGTGAAAAGGTTCTTGACACTGGTGGCCCTATCTCCGTCCCAGTT GGGAGAGAAACTTTAGGGAGAATCATCAACGTTATCGGTGAACCTATTGATGAAAGAGGT CCAATTAAGTCCAAACTAAGAAAGCCAATTCACGCAGACCCTCCTAGTTTTGCAGAACAA TCTACTTCGGCTGAAATTTTGGAAACAGGTATCAAAGTCGTCGATCTATTAGCTCCTTAT GCCAGAGGTGGTAAGATTGGTCTTTTCGGTGGTGCAGGTGTCGGTAAGACTGTGTTCATT CAAGAATTGATTAACAATATCGCCAAGGCCCATGGTGGTTTTTCCGTTTTCGCCGGTGTT GGTGAAAGGACCAGAGAGGGTAATGACTTGTACCGTGAAATGAAGGAAACTGGAGTCATT AACTTGGAAGGTGAATCCAAGGTCGCCTTAGTTTTCGGTCAAATGAACGAACCTCCAGGA GCCAGAGCCAGAGTCGCTTTAACTGGTTTGACGATCGCTGAATATTTCAGAGATGAAGAA GGTCAAGACGTCTTGTTGTTTATCGACAATATCTTTAGATTTACTCAAGCTGGTTCAGAA GTCTCTGCCCTTTTGGGTCGTATTCCATCTGCCGTCGGTTATCAACCAACTTTGGCCACT GATATGGGTCTCTTACAAGAAAGAATTACCACCACAAAGAAGGGTTCTGTCACTTCTGTG CAAGCCGTTTATGTTCCAGCCGATGATTTAACAGATCCGTCTCCGTCCACATCTTTTGCC CATTTGGACGCATCATCCGTCTTGTCAAGAGGTATTTCAGAATTAGGTATTTACCCTGCA GTGGATCCATTGGATTCTAAATCAAGGTTATTGGATGCCGCCGTTGTCGGTCAAGAACAT TATGACGTCGCCTCCAAGGTTCAAGAAACTTTACAGACCTATAAATCTTTACAAGATATC ATTGCTATTTTGGGTATGGATGAATTGTCCGAACAAGATAAACTAACTGTCGAAAGGGCA AGAAAGATTCAAAGATTCTTATCTCAACCATTTGCTGTCGCCGAAGTCTTTACTGGTATC CCAGGTAAATTAGTGAGATTAAAGGACACCGTTGCCTCGTTCAAAGCCGTTTTGGAAGGT AAATACGATAATATACCAGAACATGCTTTCTATATGGTTGGTGGTATTGAAGATGTTGTT CGTAAAGCTGAAAAGTTAGCCCGTGAAGCCAACTAG
Protein Properties
Pfam Domain Function
Protein Residues511
Protein Molecular Weight54793.30078
Protein Theoretical pI5.41
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>ATP synthase subunit beta, mitochondrial MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQ SELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY ARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI NLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSE VSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDI IAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEG KYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN
References
External Links
ResourceLink
Saccharomyces Genome Database ATP2
Uniprot IDP00830
Uniprot NameATPB_YEAST
GenBank Gene IDM12082
Genebank Protein ID171110
General Reference
  • Takeda, M., Vassarotti, A., Douglas, M. G. (1985). "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-subunit precursor." J Biol Chem 260:15458-15465.2866186
  • Liang, Y., Ackerman, S. H. (1996). "Characterization of mutations in the beta subunit of the mitochondrial F1-ATPase that produce defects in enzyme catalysis and assembly." J Biol Chem 271:26522-26528.8900121
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Walker, M. E., Valentin, E., Reid, G. A. (1990). "Transport of the yeast ATP synthase beta-subunit into mitochondria. Effects of amino acid substitutions on targeting." Biochem J 266:227-234.2138017
  • Saltzgaber-Muller, J., Kunapuli, S. P., Douglas, M. G. (1983). "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase beta subunit." J Biol Chem 258:11465-11470.6225776
  • Norbeck, J., Blomberg, A. (1996). "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." FEMS Microbiol Lett 137:1-8.8935650
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Reinders, J., Wagner, K., Zahedi, R. P., Stojanovski, D., Eyrich, B., van der Laan, M., Rehling, P., Sickmann, A., Pfanner, N., Meisinger, C. (2007). "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Mol Cell Proteomics 6:1896-1906.17761666
  • Stock, D., Leslie, A. G., Walker, J. E. (1999). "Molecular architecture of the rotary motor in ATP synthase." Science 286:1700-1705.10576729