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Q01574 (ACS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase 1

EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1
Gene names
Name:ACS1
Ordered Locus Names:YAL054C
ORF Names:FUN44
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Aerobic" isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate. Ref.6 Ref.12

Catalytic activity

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

Subcellular location

Microsome Potential. Cytoplasm. Mitochondrion. Nucleus Ref.8 Ref.9 Ref.11.

Induction

By acetate, acetaldehyde and ethanol. Subject to glucose catabolite repression. Inactivated and degraded after addition of glucose (at protein level). Ref.6 Ref.7

Miscellaneous

Present with 2890 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Caution

It is uncertain whether Met-1 or Met-25 is the initiator.

Biophysicochemical properties

Kinetic parameters:

KM=0.32 mM for acetate Ref.6

KM=1.4 mM for ATP

Vmax=1.1 µmol/min/mg enzyme

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 713713Acetyl-coenzyme A synthetase 1
PRO_0000208420

Regions

Nucleotide binding467 – 4726AMP
Motif711 – 7133Microbody targeting signal Potential

Sites

Binding site5591AMP
Binding site5741AMP

Experimental info

Sequence conflict341Q → R in CAA47054. Ref.1
Sequence conflict3281K → E in AAU09675. Ref.4

Secondary structure

........................................................................................................ 713
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01574 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: F282218B9A6CA3B2

FASTA71379,141
        10         20         30         40         50         60 
MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP QRPISDRLQP 

        70         80         90        100        110        120 
AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN WSKPFDKVFI PDPKTGRPSF 

       130        140        150        160        170        180 
QNNAWFLNGQ LNACYNCVDR HALKTPNKKA IIFEGDEPGQ GYSITYKELL EEVCQVAQVL 

       190        200        210        220        230        240 
TYSMGVRKGD TVAVYMPMVP EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV 

       250        260        270        280        290        300 
ITTDESNRGG KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY 

       310        320        330        340        350        360 
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD THQEDVFFTA 

       370        380        390        400        410        420 
GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD IIDEHKVTQF YVAPTALRLL 

       430        440        450        460        470        480 
KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV WEWYSEKIGK NEIPIVDTYW QTESGSHLVT 

       490        500        510        520        530        540 
PLAGGVTPMK PGSASFPFFG IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH 

       550        560        570        580        590        600 
DRYLDTYLNP YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI 

       610        620        630        640        650        660 
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR KDIGPFAAPK 

       670        680        690        700        710 
LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN PGIVRHLIDS VKL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae."
de Virgilio C., Buerckert N., Barth G., Neuhaus J.-M., Boller T., Wiemken A.
Yeast 8:1043-1051(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / GRF88.
[2]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[5]"Carbon source-dependent regulation of the acetyl-coenzyme A synthetase-encoding gene ACS1 from Saccharomyces cerevisiae."
Kratzer S., Schueller H.-J.
Gene 161:75-79(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
Strain: GRF78.
[6]"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.
[7]"The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose catabolite inactivation."
de Jong-Gubbels P., van den Berg M.A., Steensma H.Y., van Dijken J.P., Pronk J.T.
FEMS Microbiol. Lett. 153:75-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"Subcellular localization of the yeast proteome."
Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P., Gerstein M., Roeder G.S., Snyder M.
Genes Dev. 16:707-719(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[12]"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.
[13]"Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP."
Jogl G., Tong L.
Biochemistry 43:1425-1431(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 72-713 IN COMPLEX WITH AMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66425 Genomic DNA. Translation: CAA47054.1.
U12980 Genomic DNA. Translation: AAC04979.1.
AY723758 Genomic DNA. Translation: AAU09675.1.
X76891 Genomic DNA. Translation: CAA54220.1.
BK006935 Genomic DNA. Translation: DAA06934.1.
PIRS30019. S51967.
RefSeqNP_009347.1. NM_001178197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortalQ01574.
SMRQ01574. Positions 74-713.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31775. 37 interactions.
DIPDIP-4326N.
IntActQ01574. 4 interactions.
MINTMINT-525275.
STRING4932.YAL054C.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Proteomic databases

PaxDbQ01574.
PeptideAtlasQ01574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL054C; YAL054C; YAL054C.
GeneID851245.
KEGGsce:YAL054C.

Organism-specific databases

SGDS000000050. ACS1.

Phylogenomic databases

eggNOGCOG0365.
GeneTreeENSGT00750000117658.
HOGENOMHOG000229981.
KOK01895.
OMAPNYSRYW.
OrthoDBEOG7M3J82.

Enzyme and pathway databases

BioCycMetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
SABIO-RKQ01574.

Gene expression databases

GenevestigatorQ01574.

Family and domain databases

InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01574.
NextBio968180.
PROQ01574.

Entry information

Entry nameACS1_YEAST
AccessionPrimary (citable) accession number: Q01574
Secondary accession number(s): D6VPG4, Q66RJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references