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Protein

Acetyl-CoA acetyltransferase

Gene

ERG10

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 formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Kineticsi

  1. KM=0.16 mM for CoA1 Publication
  2. KM=0.35 mM for acetoacetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.8.1 Publication

    Pathwayi: (R)-mevalonate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Acetyl-CoA acetyltransferase (ERG10)
    2. Hydroxymethylglutaryl-CoA synthase (ERG13)
    3. 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 (HMG2), 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG1)
    This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911Acyl-thioester intermediateBy similarity
    Metal bindingi186 – 1861PotassiumBy similarity
    Binding sitei186 – 1861Coenzyme ABy similarity
    Binding sitei231 – 2311Coenzyme ABy similarity
    Metal bindingi248 – 2481Potassium; via carbonyl oxygenBy similarity
    Metal bindingi249 – 2491Potassium; via carbonyl oxygenBy similarity
    Metal bindingi251 – 2511Potassium; via carbonyl oxygenBy similarity
    Binding sitei252 – 2521Coenzyme ABy similarity
    Metal bindingi350 – 3501Potassium; via carbonyl oxygenBy similarity
    Active sitei354 – 3541Proton acceptorPROSITE-ProRule annotation
    Active sitei384 – 3841Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    • acetyl-CoA C-acetyltransferase activity Source: SGD
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • ergosterol biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Potassium

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-647.
    YEAST:YPL028W-MONOMER.
    ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.
    R-SCE-77108. Utilization of Ketone Bodies.
    R-SCE-77111. Synthesis of Ketone Bodies.
    UniPathwayiUPA00058; UER00101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase (EC:2.3.1.9)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Ergosterol biosynthesis protein 10
    Gene namesi
    Name:ERG10
    Ordered Locus Names:YPL028W
    ORF Names:LPB3
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPL028W.
    SGDiS000005949. ERG10.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources1 Publication
    Chaini2 – 398397Acetyl-CoA acetyltransferasePRO_0000206416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineCombined sources1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP41338.
    PeptideAtlasiP41338.

    PTM databases

    iPTMnetiP41338.

    Expressioni

    Inductioni

    Induced by low intracellular sterol levels.1 Publication

    Interactioni

    Subunit structurei

    Multimeric.

    Protein-protein interaction databases

    BioGridi36150. 93 interactions.
    DIPiDIP-6396N.
    IntActiP41338. 4 interactions.
    MINTiMINT-660035.

    Structurei

    3D structure databases

    ProteinModelPortaliP41338.
    SMRiP41338. Positions 3-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    InParanoidiP41338.
    KOiK00626.
    OMAiGPRNAKP.
    OrthoDBiEOG7PCJSX.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P41338-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQNVYIVST ARTPIGSFQG SLSSKTAVEL GAVALKGALA KVPELDASKD
    60 70 80 90 100
    FDEIIFGNVL SANLGQAPAR QVALAAGLSN HIVASTVNKV CASAMKAIIL
    110 120 130 140 150
    GAQSIKCGNA DVVVAGGCES MTNAPYYMPA ARAGAKFGQT VLVDGVERDG
    160 170 180 190 200
    LNDAYDGLAM GVHAEKCARD WDITREQQDN FAIESYQKSQ KSQKEGKFDN
    210 220 230 240 250
    EIVPVTIKGF RGKPDTQVTK DEEPARLHVE KLRSARTVFQ KENGTVTAAN
    260 270 280 290 300
    ASPINDGAAA VILVSEKVLK EKNLKPLAII KGWGEAAHQP ADFTWAPSLA
    310 320 330 340 350
    VPKALKHAGI EDINSVDYFE FNEAFSVVGL VNTKILKLDP SKVNVYGGAV
    360 370 380 390
    ALGHPLGCSG ARVVVTLLSI LQQEGGKIGV AAICNGGGGA SSIVIEKI
    Length:398
    Mass (Da):41,729
    Last modified:January 23, 2007 - v3
    Checksum:iE835A8E040629A5C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L20428 Genomic DNA. Translation: AAA62378.1.
    U36624 Genomic DNA. Translation: AAB68159.1.
    BK006949 Genomic DNA. Translation: DAA11401.1.
    PIRiA55654.
    RefSeqiNP_015297.1. NM_001183842.1.

    Genome annotation databases

    EnsemblFungiiYPL028W; YPL028W; YPL028W.
    GeneIDi856079.
    KEGGisce:YPL028W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L20428 Genomic DNA. Translation: AAA62378.1.
    U36624 Genomic DNA. Translation: AAB68159.1.
    BK006949 Genomic DNA. Translation: DAA11401.1.
    PIRiA55654.
    RefSeqiNP_015297.1. NM_001183842.1.

    3D structure databases

    ProteinModelPortaliP41338.
    SMRiP41338. Positions 3-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36150. 93 interactions.
    DIPiDIP-6396N.
    IntActiP41338. 4 interactions.
    MINTiMINT-660035.

    PTM databases

    iPTMnetiP41338.

    Proteomic databases

    MaxQBiP41338.
    PeptideAtlasiP41338.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYPL028W; YPL028W; YPL028W.
    GeneIDi856079.
    KEGGisce:YPL028W.

    Organism-specific databases

    EuPathDBiFungiDB:YPL028W.
    SGDiS000005949. ERG10.

    Phylogenomic databases

    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    InParanoidiP41338.
    KOiK00626.
    OMAiGPRNAKP.
    OrthoDBiEOG7PCJSX.

    Enzyme and pathway databases

    UniPathwayiUPA00058; UER00101.
    BioCyciMetaCyc:MONOMER-647.
    YEAST:YPL028W-MONOMER.
    ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.
    R-SCE-77108. Utilization of Ketone Bodies.
    R-SCE-77111. Synthesis of Ketone Bodies.

    Miscellaneous databases

    PROiP41338.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase."
      Hiser L.M., Basson M.E., Rine J.
      J. Biol. Chem. 269:31383-31389(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(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. Bienvenut W.V., Peters C.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-36 AND 137-148, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Two forms of acetoacetyl coenzyme A thiolase in yeast. I. Separation and properties."
      Kornblatt J.A., Rudney H.
      J. Biol. Chem. 246:4417-4423(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Transcriptional regulation of a sterol-biosynthetic enzyme by sterol levels in Saccharomyces cerevisiae."
      Dimster-Denk D., Rine J.
      Mol. Cell. Biol. 16:3981-3989(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTHIL_YEAST
    AccessioniPrimary (citable) accession number: P41338
    Secondary accession number(s): D6W3Y5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: June 8, 2016
    This is version 152 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 60895 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.