Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A synthetase 2

Gene

ACS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.

Kineticsi

  1. KM=8.8 mM for acetate1 Publication
  2. KM=1.3 mM for ATP1 Publication
  1. Vmax=0.34 µmol/min/mg enzyme1 Publication

Pathwayi: pyruvate metabolism

This protein is involved in the pathway pyruvate metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway pyruvate metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei325 – 3251Coenzyme ABy similarity
Binding sitei516 – 5161AMPBy similarity
Binding sitei516 – 5161ATPBy similarity
Binding sitei531 – 5311AMPBy similarity
Binding sitei531 – 5311ATPBy similarity
Binding sitei539 – 5391Coenzyme A; via carbonyl oxygenBy similarity
Binding sitei542 – 5421ATPBy similarity
Binding sitei612 – 6121Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033ATPBy similarity
Nucleotide bindingi425 – 4306AMPBy similarity
Nucleotide bindingi425 – 4306ATPBy similarity

GO - Molecular functioni

  • acetate-CoA ligase activity Source: SGD
  • acid-ammonia (or amide) ligase activity Source: SGD
  • AMP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • acetyl-CoA biosynthetic process Source: SGD
  • acetyl-CoA biosynthetic process from acetate Source: InterPro
  • histone acetylation Source: SGD
  • pyruvate metabolic process Source: UniProtKB-UniPathway
  • replicative cell aging Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YLR153C-MONOMER.
YEAST:YLR153C-MONOMER.
ReactomeiR-SCE-77111. Synthesis of Ketone Bodies.
SABIO-RKP52910.
UniPathwayiUPA00231.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 2 (EC:6.2.1.1)
Alternative name(s):
Acetate--CoA ligase 2
Acyl-activating enzyme 2
Gene namesi
Name:ACS2
Ordered Locus Names:YLR153C
ORF Names:L9634.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR153C.
SGDiS000004143. ACS2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleolus Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Acetyl-coenzyme A synthetase 2PRO_0000208421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki506 – 506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei679 – 6791PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP52910.
PeptideAtlasiP52910.

PTM databases

iPTMnetiP52910.

Interactioni

Protein-protein interaction databases

BioGridi31422. 190 interactions.
DIPiDIP-992N.
IntActiP52910. 42 interactions.
MINTiMINT-548498.

Structurei

3D structure databases

ProteinModelPortaliP52910.
SMRiP52910. Positions 38-674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 2094Coenzyme A bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiP52910.
KOiK01895.
OMAiGSVCAPK.
OrthoDBiEOG7M3J82.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIKEHKVVY EAHNVKALKA PQHFYNSQPG KGYVTDMQHY QEMYQQSINE
60 70 80 90 100
PEKFFDKMAK EYLHWDAPYT KVQSGSLNNG DVAWFLNGKL NASYNCVDRH
110 120 130 140 150
AFANPDKPAL IYEADDESDN KIITFGELLR KVSQIAGVLK SWGVKKGDTV
160 170 180 190 200
AIYLPMIPEA VIAMLAVARI GAIHSVVFAG FSAGSLKDRV VDANSKVVIT
210 220 230 240 250
CDEGKRGGKT INTKKIVDEG LNGVDLVSRI LVFQRTGTEG IPMKAGRDYW
260 270 280 290 300
WHEEAAKQRT YLPPVSCDAE DPLFLLYTSG STGSPKGVVH TTGGYLLGAA
310 320 330 340 350
LTTRYVFDIH PEDVLFTAGD VGWITGHTYA LYGPLTLGTA SIIFESTPAY
360 370 380 390 400
PDYGRYWRII QRHKATHFYV APTALRLIKR VGEAEIAKYD TSSLRVLGSV
410 420 430 440 450
GEPISPDLWE WYHEKVGNKN CVICDTMWQT ESGSHLIAPL AGAVPTKPGS
460 470 480 490 500
ATVPFFGINA CIIDPVTGVE LEGNDVEGVL AVKSPWPSMA RSVWNHHDRY
510 520 530 540 550
MDTYLKPYPG HYFTGDGAGR DHDGYYWIRG RVDDVVNVSG HRLSTSEIEA
560 570 580 590 600
SISNHENVSE AAVVGIPDEL TGQTVVAYVS LKDGYLQNNA TEGDAEHITP
610 620 630 640 650
DNLRRELILQ VRGEIGPFAS PKTIILVRDL PRTRSGKIMR RVLRKVASNE
660 670 680
AEQLGDLTTL ANPEVVPAII SAVENQFFSQ KKK
Length:683
Mass (Da):75,492
Last modified:October 1, 1996 - v1
Checksum:i418439EDCDF308F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79456 Genomic DNA. Translation: AAB35143.1.
U53879 Genomic DNA. Translation: AAB82387.1.
Z73325 Genomic DNA. Translation: CAA97725.1.
BK006945 Genomic DNA. Translation: DAA09464.1.
PIRiS65002.
RefSeqiNP_013254.1. NM_001182040.1.

Genome annotation databases

EnsemblFungiiYLR153C; YLR153C; YLR153C.
GeneIDi850846.
KEGGisce:YLR153C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79456 Genomic DNA. Translation: AAB35143.1.
U53879 Genomic DNA. Translation: AAB82387.1.
Z73325 Genomic DNA. Translation: CAA97725.1.
BK006945 Genomic DNA. Translation: DAA09464.1.
PIRiS65002.
RefSeqiNP_013254.1. NM_001182040.1.

3D structure databases

ProteinModelPortaliP52910.
SMRiP52910. Positions 38-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31422. 190 interactions.
DIPiDIP-992N.
IntActiP52910. 42 interactions.
MINTiMINT-548498.

PTM databases

iPTMnetiP52910.

Proteomic databases

MaxQBiP52910.
PeptideAtlasiP52910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR153C; YLR153C; YLR153C.
GeneIDi850846.
KEGGisce:YLR153C.

Organism-specific databases

EuPathDBiFungiDB:YLR153C.
SGDiS000004143. ACS2.

Phylogenomic databases

GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiP52910.
KOiK01895.
OMAiGSVCAPK.
OrthoDBiEOG7M3J82.

Enzyme and pathway databases

UniPathwayiUPA00231.
BioCyciMetaCyc:YLR153C-MONOMER.
YEAST:YLR153C-MONOMER.
ReactomeiR-SCE-77111. Synthesis of Ketone Bodies.
SABIO-RKP52910.

Miscellaneous databases

PROiP52910.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-506.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACS2_YEAST
AccessioniPrimary (citable) accession number: P52910
Secondary accession number(s): D6VYE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 225000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.