UniProt Accession

 ACS2_YEAST; P52910; D6VYE8 

Genbank Protein ID

 S79456; U53879; Z73325; BK006945 

Genbank Nucleotide ID

 AAB35143.1; AAB82387.1; CAA97725.1; DAA09464.1 

Protein Name

 Acetyl-coenzyme A synthetase 2 

Protein Synonyms/Alias

 Acetate--CoA ligase 2; Acyl-activating enzyme 2 

Gene Name

 ACS2 

Gene Synonyms/Alias

 YLR153C; L9634.10 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
7	*MTIKEHKVVYEAHN	acetylation	[1]
16	VYEAHNVKALKAPQH	acetylation	[1]
19	AHNVKALKAPQHFYN	acetylation	[1]
107	HAFANPDKPALIYEA	acetylation	[1]
205	VITCDEGKRGGKTIN	acetylation	[1]
205	VITCDEGKRGGKTIN	ubiquitination	[2]
215	GKTINTKKIVDEGLN	acetylation	[1]
388	VGEAEIAKYDTSSLR	acetylation	[1]
388	VGEAEIAKYDTSSLR	ubiquitination	[2]
506	RYMDTYLKPYPGHYF	acetylation	[1]
506	RYMDTYLKPYPGHYF	ubiquitination	[3, 4, 5]
622	IGPFASPKTIILVRD	acetylation	[1]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [4] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [5] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269] 

Functional Description

 Catalyzes 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. 

Sequence Annotation

 NP_BIND 425 430 AMP (By similarity).
 BINDING 516 516 AMP (By similarity).
 BINDING 531 531 AMP (By similarity).
 MOD_RES 679 679 Phosphoserine.
 CROSSLNK 506 506 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 ATP-binding; Complete proteome; Cytoplasm; Isopeptide bond; Ligase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 683 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0003987; F:acetate-CoA ligase activity; IDA:SGD.
 GO:0016880; F:acid-ammonia (or amide) ligase activity; IDA:SGD.
 GO:0016208; F:AMP binding; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006085; P:acetyl-CoA biosynthetic process; IDA:SGD.
 GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
 GO:0016573; P:histone acetylation; IMP:SGD.
 GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniPathway.
 GO:0001302; P:replicative cell aging; IMP:SGD. 

Interpro

 IPR011904; Ac_CoA_lig.
 IPR024597; Acyl-CoA_synth_DUF3448.
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 

Pfam

 PF00501; AMP-binding
 PF11930; DUF3448
 PF13193; DUF4009 

SMART

  

PROSITE

 PS00455; AMP_BINDING 

PRINTS