Acetyl-coenzyme A synthetase 2 (P52910)

Identification
NameAcetyl-coenzyme A synthetase 2
Synonyms
  • Acetate--CoA ligase 2
  • Acyl-activating enzyme 2
Gene NameACS2
Enzyme Class
Biological Properties
General FunctionInvolved in acetate-CoA ligase activity
Specific FunctionCatalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Anaerobic" isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass
Cellular LocationCytoplasm. Nucleus.
SMPDB Pathways
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycolysis / Gluconeogenesisec00010 Map00010
Methane metabolismec00680 Map00680
Propanoate metabolismec00640 Map00640
Pyruvate metabolismec00620 Map00620
SMPDB Reactions
Acetyl-CoA + Adenosine monophosphate ↔ Coenzyme A + Acetyl adenylate
Acetyl adenylate + Pyrophosphate ↔ Acetic acid + Adenosine triphosphate
KEGG Reactions
Adenosine triphosphate + Acetic acid + Coenzyme A → Adenosine monophosphate + Pyrophosphate + Acetyl-CoA
Adenosine triphosphate + Acetic acid + Coenzyme A ↔ Adenosine monophosphate + Pyrophosphate + Acetyl-CoA
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00056Acetic acidShow
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00312Acetyl-CoAShow
YMDB00446propionyl-CoAShow
YMDB00857propionic acidShow
YMDB16193Acetyl adenylateShow
GO Classification
Component
Not Available
Function
adenyl ribonucleotide binding
ligase activity, forming carbon-sulfur bonds
CoA-ligase activity
AMP binding
acetate-CoA ligase activity
catalytic activity
ligase activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLR153C
Gene Sequence>2052 bp ATGACAATCAAGGAACATAAAGTAGTTTATGAAGCTCACAACGTAAAGGCTCTTAAGGCT CCTCAACATTTTTACAACAGCCAACCCGGCAAGGGTTACGTTACTGATATGCAACATTAT CAAGAAATGTATCAACAATCTATCAATGAGCCAGAAAAATTCTTTGATAAGATGGCTAAG GAATACTTGCATTGGGATGCTCCATACACCAAAGTTCAATCTGGTTCATTGAACAATGGT GATGTTGCATGGTTTTTGAACGGTAAATTGAATGCATCATACAATTGTGTTGACAGACAT GCCTTTGCTAATCCCGACAAGCCAGCTTTGATCTATGAAGCTGATGACGAATCCGACAAC AAAATCATCACATTTGGTGAATTACTCAGAAAAGTTTCCCAAATCGCTGGTGTCTTAAAA AGCTGGGGCGTTAAGAAAGGTGACACAGTGGCTATCTATTTGCCAATGATTCCAGAAGCG GTCATTGCTATGTTGGCTGTGGCTCGTATTGGTGCTATTCACTCTGTTGTCTTTGCTGGG TTCTCCGCTGGTTCGTTGAAAGATCGTGTCGTTGACGCTAATTCTAAAGTGGTCATCACT TGTGATGAAGGTAAAAGAGGTGGTAAGACCATCAACACTAAAAAAATTGTTGACGAAGGT TTGAACGGAGTCGATTTGGTTTCCCGTATCTTGGTTTTCCAAAGAACTGGTACTGAAGGT ATTCCAATGAAGGCCGGTAGAGATTACTGGTGGCATGAGGAGGCCGCTAAGCAGAGAACT TACCTACCTCCTGTTTCATGTGACGCTGAAGATCCTCTATTTTTATTATACACTTCCGGT TCCACTGGTTCTCCAAAGGGTGTCGTTCACACTACAGGTGGTTATTTATTAGGTGCCGCT TTAACAACTAGATACGTTTTTGATATTCACCCAGAAGATGTTCTCTTCACTGCCGGTGAC GTCGGCTGGATCACGGGTCACACCTATGCTCTATATGGTCCATTAACCTTGGGTACCGCC TCAATAATTTTCGAATCCACTCCTGCCTACCCAGATTATGGTAGATATTGGAGAATTATC CAACGTCACAAGGCTACCCATTTCTATGTGGCTCCAACTGCTTTAAGATTAATCAAACGT GTAGGTGAAGCCGAAATTGCCAAATATGACACTTCCTCATTACGTGTCTTGGGTTCCGTC GGTGAACCAATCTCTCCAGACTTATGGGAATGGTATCATGAAAAAGTGGGTAACAAAAAC TGTGTCATTTGTGACACTATGTGGCAAACAGAGTCTGGTTCTCATTTAATTGCTCCTTTG GCAGGTGCTGTCCCAACAAAACCTGGTTCTGCTACCGTGCCATTCTTTGGTATTAACGCT TGTATCATTGACCCTGTTACAGGTGTGGAATTAGAAGGTAATGATGTCGAAGGTGTCCTT GCCGTTAAATCACCATGGCCATCAATGGCTAGATCTGTTTGGAACCACCACGACCGTTAC ATGGATACTTACTTGAAACCTTATCCTGGTCACTATTTCACAGGTGATGGTGCTGGTAGA GATCATGATGGTTACTACTGGATCAGGGGTAGAGTTGACGACGTTGTAAATGTTTCCGGT CATAGATTATCCACATCAGAAATTGAAGCATCTATCTCAAATCACGAAAACGTCTCGGAA GCTGCTGTTGTCGGTATTCCAGATGAATTGACCGGTCAAACCGTCGTTGCATATGTTTCC CTAAAAGATGGTTATCTACAAAACAACGCTACTGAAGGTGATGCAGAACACATCACACCA GATAATTTACGTAGAGAATTGATCTTACAAGTTAGGGGTGAGATTGGTCCTTTCGCCTCA CCAAAAACCATTATTCTAGTTAGAGATCTACCAAGAACAAGGTCAGGAAAGATTATGAGA AGAGTTCTAAGAAAGGTTGCTTCTAACGAAGCCGAACAGCTAGGTGACCTAACTACTTTG GCCAACCCAGAAGTTGTACCTGCCATCATTTCTGCTGTAGAGAACCAATTTTTCTCTCAA AAAAAGAAATAA
Protein Properties
Pfam Domain Function
Protein Residues683
Protein Molecular Weight75491.10156
Protein Theoretical pI6.67
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Acetyl-coenzyme A synthetase 2 MTIKEHKVVYEAHNVKALKAPQHFYNSQPGKGYVTDMQHYQEMYQQSINEPEKFFDKMAK EYLHWDAPYTKVQSGSLNNGDVAWFLNGKLNASYNCVDRHAFANPDKPALIYEADDESDN KIITFGELLRKVSQIAGVLKSWGVKKGDTVAIYLPMIPEAVIAMLAVARIGAIHSVVFAG FSAGSLKDRVVDANSKVVITCDEGKRGGKTINTKKIVDEGLNGVDLVSRILVFQRTGTEG IPMKAGRDYWWHEEAAKQRTYLPPVSCDAEDPLFLLYTSGSTGSPKGVVHTTGGYLLGAA LTTRYVFDIHPEDVLFTAGDVGWITGHTYALYGPLTLGTASIIFESTPAYPDYGRYWRII QRHKATHFYVAPTALRLIKRVGEAEIAKYDTSSLRVLGSVGEPISPDLWEWYHEKVGNKN CVICDTMWQTESGSHLIAPLAGAVPTKPGSATVPFFGINACIIDPVTGVELEGNDVEGVL AVKSPWPSMARSVWNHHDRYMDTYLKPYPGHYFTGDGAGRDHDGYYWIRGRVDDVVNVSG HRLSTSEIEASISNHENVSEAAVVGIPDELTGQTVVAYVSLKDGYLQNNATEGDAEHITP DNLRRELILQVRGEIGPFASPKTIILVRDLPRTRSGKIMRRVLRKVASNEAEQLGDLTTL ANPEVVPAIISAVENQFFSQKKK
References
External Links
ResourceLink
Saccharomyces Genome Database ACS2
Uniprot IDP52910
Uniprot NameACS2_YEAST
GenBank Gene IDS79456
Genebank Protein ID1168014
General Reference
  • Van den Berg, M. A., Steensma, H. Y. (1995). "ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose." Eur J Biochem 231:704-713.7649171
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • van den Berg, M. A., de Jong-Gubbels, P., Kortland, C. J., van Dijken, J. P., Pronk, J. T., Steensma, H. Y. (1996). "The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation." J Biol Chem 271:28953-28959.8910545
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Takahashi, H., McCaffery, J. M., Irizarry, R. A., Boeke, J. D. (2006). "Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription." Mol Cell 23:207-217.16857587
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956