P52910 (ACS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase 2
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase 2
Acyl-activating enzyme 2

Gene names

Name:	ACS2
Ordered Locus Names:	YLR153C
ORF Names:	L9634.10

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	683 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.8
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
Pathway	Carbohydrate metabolism; pyruvate metabolism.
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly nuclear. Ref.5 Ref.8
Miscellaneous	Present with 225000 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Biophysicochemical properties	Kinetic parameters: KM=8.8 mM for acetate Ref.4 KM=1.3 mM for ATP Vmax=0.34 µmol/min/mg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process Inferred from direct assay Ref.4. Source: SGD histone acetylation Inferred from mutant phenotype Ref.8. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay Ref.8. Source: SGD nucleolus Inferred from direct assay. Source: SGD
Molecular function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from direct assay Ref.4. Source: SGD acid-ammonia (or amide) ligase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 683	683	Acetyl-coenzyme A synthetase 2		PRO_0000208421
Regions
	Nucleotide binding	425 – 430	6	AMP By similarity
Sites
	Binding site	516	1	AMP By similarity
	Binding site	531	1	AMP By similarity
Amino acid modifications
	Modified residue	620	1	Phosphoserine Ref.9
	Modified residue	679	1	Phosphoserine Ref.9
	Cross-link	506		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P52910 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 418439EDCDF308F3	FASTA	683	75,492
	10 20 30 40 50 60 MTIKEHKVVY EAHNVKALKA PQHFYNSQPG KGYVTDMQHY QEMYQQSINE PEKFFDKMAK 70 80 90 100 110 120 EYLHWDAPYT KVQSGSLNNG DVAWFLNGKL NASYNCVDRH AFANPDKPAL IYEADDESDN 130 140 150 160 170 180 KIITFGELLR KVSQIAGVLK SWGVKKGDTV AIYLPMIPEA VIAMLAVARI GAIHSVVFAG 190 200 210 220 230 240 FSAGSLKDRV VDANSKVVIT CDEGKRGGKT INTKKIVDEG LNGVDLVSRI LVFQRTGTEG 250 260 270 280 290 300 IPMKAGRDYW WHEEAAKQRT YLPPVSCDAE DPLFLLYTSG STGSPKGVVH TTGGYLLGAA 310 320 330 340 350 360 LTTRYVFDIH PEDVLFTAGD VGWITGHTYA LYGPLTLGTA SIIFESTPAY PDYGRYWRII 370 380 390 400 410 420 QRHKATHFYV APTALRLIKR VGEAEIAKYD TSSLRVLGSV GEPISPDLWE WYHEKVGNKN 430 440 450 460 470 480 CVICDTMWQT ESGSHLIAPL AGAVPTKPGS ATVPFFGINA CIIDPVTGVE LEGNDVEGVL 490 500 510 520 530 540 AVKSPWPSMA RSVWNHHDRY MDTYLKPYPG HYFTGDGAGR DHDGYYWIRG RVDDVVNVSG 550 560 570 580 590 600 HRLSTSEIEA SISNHENVSE AAVVGIPDEL TGQTVVAYVS LKDGYLQNNA TEGDAEHITP 610 620 630 640 650 660 DNLRRELILQ VRGEIGPFAS PKTIILVRDL PRTRSGKIMR RVLRKVASNE AEQLGDLTTL 670 680 ANPEVVPAII SAVENQFFSQ KKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose." van den Berg M.A., de Steensma H.Y. Eur. J. Biochem. 231:704-713(1995) [PubMed: 7649171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The two acetyl-coenzyme A synthetases of Saccharomyces cerevisiae differ with respect to kinetic properties and transcriptional regulation." van den Berg M.A., de Jong-Gubbels P., Kortland C.J., van Dijken J.P., Pronk J.T., Steensma H.Y. J. Biol. Chem. 271:28953-28959(1996) [PubMed: 8910545] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-506, MASS SPECTROMETRY. Strain: SUB592.
[8]	"Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription." Takahashi H., McCaffery J.M., Irizarry R.A., Boeke J.D. Mol. Cell 23:207-217(2006) [PubMed: 16857587] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620 AND SER-679, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S79456 Genomic DNA. Translation: AAB35143.1. U53879 Genomic DNA. Translation: AAB82387.1. Z73325 Genomic DNA. Translation: CAA97725.1. BK006945 Genomic DNA. Translation: DAA09464.1.
PIR	S65002.
RefSeq	NP_013254.1. NM_001182040.1.
3D structure databases
ProteinModelPortal	P52910.
SMR	P52910. Positions 38-674.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-992N.
IntAct	P52910. 42 interactions.
MINT	MINT-548498.
STRING	P52910.
Proteomic databases
PeptideAtlas	P52910.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR153C; YLR153C; YLR153C.
GeneID	850846.
KEGG	sce:YLR153C.
NMPDR	fig|4932.3.peg.4248.
Organism-specific databases
CYGD	YLR153c.
SGD	S000004143. ACS2.
Phylogenomic databases
eggNOG	fuNOG05220.
GeneTree	EFGT00050000001162.
HOGENOM	HBG547964.
OMA	DYWWHEE.
OrthoDB	EOG4M0J8W.
Gene expression databases
ArrayExpress	P52910.
Genevestigator	P52910.
GermOnline	YLR153C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01895.
PANTHER	PTHR24095:SF42. PTHR24095:SF42. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967138.

Entry information

Entry name

ACS2_YEAST

Accession

Primary (citable) accession number: P52910
Secondary accession number(s): D6VYE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program