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 1

Gene

ACS1

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. "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.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.32 mM for acetate1 Publication
  2. KM=1.4 mM for ATP1 Publication
  1. Vmax=1.1 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei367 – 3671Coenzyme ABy similarity
Binding sitei559 – 5591ATP
Binding sitei574 – 5741ATP
Binding sitei582 – 5821Coenzyme A; via carbonyl oxygenBy similarity
Binding sitei585 – 5851ATPBy similarity
Binding sitei650 – 6501Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi443 – 4453ATP
Nucleotide bindingi467 – 4726ATP

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

  • acetate fermentation Source: SGD
  • acetyl-CoA biosynthetic process Source: SGD
  • acetyl-CoA biosynthetic process from acetate Source: InterPro
  • histone acetylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
BRENDAi6.2.1.1. 984.
ReactomeiREACT_279386. Ethanol oxidation.
SABIO-RKQ01574.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 1 (EC:6.2.1.1)
Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1
Gene namesi
Name:ACS1
Ordered Locus Names:YAL054C
ORF Names:FUN44
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL054C.
SGDiS000000050. ACS1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • endoplasmic reticulum Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Acetyl-coenzyme A synthetase 1PRO_0000208420Add
BLAST

Proteomic databases

MaxQBiQ01574.
PaxDbiQ01574.
PeptideAtlasiQ01574.

Expressioni

Inductioni

By acetate, acetaldehyde and ethanol. Subject to glucose catabolite repression. Inactivated and degraded after addition of glucose (at protein level).2 Publications

Interactioni

Protein-protein interaction databases

BioGridi31775. 39 interactions.
DIPiDIP-4326N.
IntActiQ01574. 4 interactions.
MINTiMINT-525275.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 8511Combined sources
Helixi87 – 9812Combined sources
Beta strandi113 – 1153Combined sources
Helixi133 – 1375Combined sources
Helixi139 – 1424Combined sources
Beta strandi148 – 1547Combined sources
Beta strandi162 – 1654Combined sources
Helixi166 – 18217Combined sources
Beta strandi191 – 1944Combined sources
Helixi200 – 21112Combined sources
Beta strandi215 – 2184Combined sources
Helixi225 – 23511Combined sources
Beta strandi238 – 2458Combined sources
Helixi255 – 2628Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi287 – 2926Combined sources
Helixi293 – 2975Combined sources
Beta strandi316 – 3205Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi328 – 3325Combined sources
Helixi335 – 34814Combined sources
Beta strandi356 – 3594Combined sources
Helixi366 – 3716Combined sources
Helixi374 – 3796Combined sources
Beta strandi381 – 3866Combined sources
Helixi397 – 4048Combined sources
Beta strandi408 – 4125Combined sources
Helixi414 – 4207Combined sources
Beta strandi427 – 4304Combined sources
Beta strandi438 – 4414Combined sources
Helixi448 – 4569Combined sources
Beta strandi461 – 4633Combined sources
Beta strandi465 – 4673Combined sources
Turni472 – 4743Combined sources
Beta strandi478 – 4803Combined sources
Turni483 – 4853Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi508 – 5103Combined sources
Beta strandi520 – 5278Combined sources
Helixi540 – 5478Combined sources
Beta strandi549 – 5513Combined sources
Beta strandi554 – 56310Combined sources
Beta strandi569 – 5713Combined sources
Beta strandi581 – 5833Combined sources
Helixi588 – 5969Combined sources
Beta strandi601 – 6077Combined sources
Beta strandi619 – 6246Combined sources
Helixi641 – 65212Combined sources
Turni655 – 6573Combined sources
Beta strandi660 – 6645Combined sources
Helixi678 – 6836Combined sources
Helixi702 – 7098Combined sources
Turni710 – 7123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortaliQ01574.
SMRiQ01574. Positions 74-713.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01574.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 2514Coenzyme A bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi711 – 7133Microbody targeting signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiQ01574.
KOiK01895.
OMAiPRIPELY.
OrthoDBiEOG7M3J82.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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.

Q01574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP
60 70 80 90 100
QRPISDRLQP AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN
110 120 130 140 150
WSKPFDKVFI PDPKTGRPSF QNNAWFLNGQ LNACYNCVDR HALKTPNKKA
160 170 180 190 200
IIFEGDEPGQ GYSITYKELL EEVCQVAQVL TYSMGVRKGD TVAVYMPMVP
210 220 230 240 250
EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV ITTDESNRGG
260 270 280 290 300
KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY
310 320 330 340 350
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD
360 370 380 390 400
THQEDVFFTA GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD
410 420 430 440 450
IIDEHKVTQF YVAPTALRLL KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV
460 470 480 490 500
WEWYSEKIGK NEIPIVDTYW QTESGSHLVT PLAGGVTPMK PGSASFPFFG
510 520 530 540 550
IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH DRYLDTYLNP
560 570 580 590 600
YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI
610 620 630 640 650
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR
660 670 680 690 700
KDIGPFAAPK LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN
710
PGIVRHLIDS VKL
Length:713
Mass (Da):79,141
Last modified:September 1, 2009 - v2
Checksum:iF282218B9A6CA3B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341Q → R in CAA47054 (PubMed:1363452).Curated
Sequence conflicti328 – 3281K → E in AAU09675 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51967. S30019.
RefSeqiNP_009347.1. NM_001178197.1.

Genome annotation databases

EnsemblFungiiYAL054C; YAL054C; YAL054C.
GeneIDi851245.
KEGGisce:YAL054C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51967. S30019.
RefSeqiNP_009347.1. NM_001178197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortaliQ01574.
SMRiQ01574. Positions 74-713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31775. 39 interactions.
DIPiDIP-4326N.
IntActiQ01574. 4 interactions.
MINTiMINT-525275.

Proteomic databases

MaxQBiQ01574.
PaxDbiQ01574.
PeptideAtlasiQ01574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL054C; YAL054C; YAL054C.
GeneIDi851245.
KEGGisce:YAL054C.

Organism-specific databases

EuPathDBiFungiDB:YAL054C.
SGDiS000000050. ACS1.

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
InParanoidiQ01574.
KOiK01895.
OMAiPRIPELY.
OrthoDBiEOG7M3J82.

Enzyme and pathway databases

BioCyciMetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
BRENDAi6.2.1.1. 984.
ReactomeiREACT_279386. Ethanol oxidation.
SABIO-RKQ01574.

Miscellaneous databases

EvolutionaryTraceiQ01574.
NextBioi968180.
PROiQ01574.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: SUBCELLULAR LOCATION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. 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 THE ATP ANALOG AMP.

Entry informationi

Entry nameiACS1_YEAST
AccessioniPrimary (citable) accession number: Q01574
Secondary accession number(s): D6VPG4, Q66RJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 1, 2009
Last modified: July 22, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2890 molecules/cell in log phase SD medium.1 Publication

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

External Data

Dasty 3

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 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.