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Q01574

- ACS1_YEAST

UniProt

Q01574 - ACS1_YEAST

Protein

Acetyl-coenzyme A synthetase 1

Gene

ACS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Sep 2009)
      Previous versions | rss
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    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

    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

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

    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

    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-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: Chromosome I

    Organism-specific databases

    SGDiS000000050. ACS1.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    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

    1
    713
    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.
    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.
    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

    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:
    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...
    MobiDBi Search...

    Protein-protein interaction databases

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

    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-RK 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

    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: October 1, 2014
    This is version 136 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