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Q01574

- ACS1_YEAST

UniProt

Q01574 - ACS1_YEAST

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Protein
Acetyl-coenzyme A synthetase 1
Gene
ACS1, YAL054C, FUN44
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 ATP

Vmax=1.1 µmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei559 – 5591AMP
Binding sitei574 – 5741AMP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi467 – 4726AMP

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: SGD
  4. acid-ammonia (or amide) ligase activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. acetate fermentation Source: SGD
  2. acetyl-CoA biosynthetic process Source: SGD
  3. acetyl-CoA biosynthetic process from acetate Source: InterPro
  4. 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.
ReactomeiREACT_86838. Ethanol oxidation.
SABIO-RKiQ01574.

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: Chromosome I

Organism-specific databases

SGDiS000000050. ACS1.

Subcellular locationi

Microsome Reviewed prediction. Cytoplasm. Mitochondrion. Nucleus 3 Publications

GO - Cellular componenti

  1. cytosol Source: SGD
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. mitochondrion Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

Pathology & Biotechi

PTM / Processingi

Molecule processing

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

Gene expression databases

GenevestigatoriQ01574.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SRP1Q028211EBI-2128,EBI-1797
YAT1P802351EBI-2128,EBI-3928
YLR049CQ121101EBI-2128,EBI-33635

Protein-protein interaction databases

BioGridi31775. 37 interactions.
DIPiDIP-4326N.
IntActiQ01574. 4 interactions.
MINTiMINT-525275.
STRINGi4932.YAL054C.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY2X-ray2.30A72-713[»]
ProteinModelPortaliQ01574.
SMRiQ01574. Positions 74-713.

Miscellaneous databases

EvolutionaryTraceiQ01574.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi711 – 7133Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00750000117658.
HOGENOMiHOG000229981.
KOiK01895.
OMAiHPPQKML.
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

MSPSAVQSSK LEEQSSEIDK LKAKMSQSAA TAQQKKEHEY EHLTSVKIVP    50
QRPISDRLQP AIATHYSPHL DGLQDYQRLH KESIEDPAKF FGSKATQFLN 100
WSKPFDKVFI PDPKTGRPSF QNNAWFLNGQ LNACYNCVDR HALKTPNKKA 150
IIFEGDEPGQ GYSITYKELL EEVCQVAQVL TYSMGVRKGD TVAVYMPMVP 200
EAIITLLAIS RIGAIHSVVF AGFSSNSLRD RINDGDSKVV ITTDESNRGG 250
KVIETKRIVD DALRETPGVR HVLVYRKTNN PSVAFHAPRD LDWATEKKKY 300
KTYYPCTPVD SEDPLFLLYT SGSTGAPKGV QHSTAGYLLG ALLTMRYTFD 350
THQEDVFFTA GDIGWITGHT YVVYGPLLYG CATLVFEGTP AYPNYSRYWD 400
IIDEHKVTQF YVAPTALRLL KRAGDSYIEN HSLKSLRCLG SVGEPIAAEV 450
WEWYSEKIGK NEIPIVDTYW QTESGSHLVT PLAGGVTPMK PGSASFPFFG 500
IDAVVLDPNT GEELNTSHAE GVLAVKAAWP SFARTIWKNH DRYLDTYLNP 550
YPGYYFTGDG AAKDKDGYIW ILGRVDDVVN VSGHRLSTAE IEAAIIEDPI 600
VAECAVVGFN DDLTGQAVAA FVVLKNKSSW STATDDELQD IKKHLVFTVR 650
KDIGPFAAPK LIILVDDLPK TRSGKIMRRI LRKILAGESD QLGDVSTLSN 700
PGIVRHLIDS VKL 713
Length:713
Mass (Da):79,141
Last modified:September 1, 2009 - v2
Checksum:iF282218B9A6CA3B2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341Q → R in CAA47054. 1 Publication
Sequence conflicti328 – 3281K → E in AAU09675. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S51967. S30019.
RefSeqi NP_009347.1. NM_001178197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RY2 X-ray 2.30 A 72-713 [» ]
ProteinModelPortali Q01574.
SMRi Q01574. Positions 74-713.
ModBasei Search...

Protein-protein interaction databases

BioGridi 31775. 37 interactions.
DIPi DIP-4326N.
IntActi Q01574. 4 interactions.
MINTi MINT-525275.
STRINGi 4932.YAL054C.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

Proteomic databases

MaxQBi Q01574.
PaxDbi Q01574.
PeptideAtlasi Q01574.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL054C ; YAL054C ; YAL054C .
GeneIDi 851245.
KEGGi sce:YAL054C.

Organism-specific databases

SGDi S000000050. ACS1.

Phylogenomic databases

eggNOGi COG0365.
GeneTreei ENSGT00750000117658.
HOGENOMi HOG000229981.
KOi K01895.
OMAi HPPQKML.
OrthoDBi EOG7M3J82.

Enzyme and pathway databases

BioCyci MetaCyc:YAL054C-MONOMER.
YEAST:YAL054C-MONOMER.
Reactomei REACT_86838. Ethanol oxidation.
SABIO-RKi Q01574.

Miscellaneous databases

EvolutionaryTracei Q01574.
NextBioi 968180.
PROi Q01574.

Gene expression databases

Genevestigatori Q01574.

Family and domain databases

InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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: September 3, 2014
This is version 135 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.

Caution

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

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

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