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P27796

- THIK_YEAST

UniProt

P27796 - THIK_YEAST

Protein

3-ketoacyl-CoA thiolase, peroxisomal

Gene

POT1

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 141 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei125 – 1251Acyl-thioester intermediate
    Active sitei375 – 3751Proton acceptor
    Active sitei403 – 4031Proton acceptor

    GO - Molecular functioni

    1. acetyl-CoA C-acyltransferase activity Source: SGD
    2. mRNA binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. fatty acid beta-oxidation Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:YIL160C-MONOMER.
    YEAST:YIL160C-MONOMER.
    ReactomeiREACT_188947. alpha-linolenic acid (ALA) metabolism.
    UniPathwayiUPA00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase, peroxisomal (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Peroxisomal 3-oxoacyl-CoA thiolase
    Gene namesi
    Name:POT1
    Synonyms:FOX3, POX3
    Ordered Locus Names:YIL160C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIL160c.
    SGDiS000001422. POT1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: SGD
    2. peroxisomal matrix Source: SGD
    3. peroxisome Source: SGD

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 4173-ketoacyl-CoA thiolase, peroxisomalPRO_0000034078
    Transit peptidei1 – ?Peroxisome

    Proteomic databases

    PaxDbiP27796.
    PeptideAtlasiP27796.

    2D gel databases

    UCD-2DPAGEP27796.

    Expressioni

    Gene expression databases

    GenevestigatoriP27796.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PEX7P391083EBI-19236,EBI-13183

    Protein-protein interaction databases

    BioGridi34832. 69 interactions.
    DIPiDIP-1504N.
    IntActiP27796. 3 interactions.
    MINTiMINT-412295.
    STRINGi4932.YIL160C.

    Structurei

    Secondary structure

    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1515
    Turni26 – 294
    Beta strandi36 – 438
    Turni49 – 513
    Turni53 – 564
    Helixi59 – 7214
    Helixi76 – 794
    Helixi82 – 843
    Beta strandi88 – 914
    Beta strandi93 – 964
    Helixi97 – 993
    Helixi100 – 10910
    Beta strandi118 – 1225
    Helixi124 – 1263
    Helixi127 – 14014
    Beta strandi145 – 15410
    Helixi155 – 1584
    Helixi159 – 1613
    Helixi162 – 1643
    Helixi171 – 1755
    Helixi179 – 1835
    Helixi186 – 19611
    Helixi201 – 22020
    Turni225 – 2273
    Helixi251 – 2555
    Turni270 – 2723
    Beta strandi276 – 28712
    Helixi288 – 2936
    Beta strandi300 – 30910
    Helixi312 – 3176
    Helixi318 – 33013
    Helixi334 – 3363
    Beta strandi338 – 3425
    Helixi347 – 35711
    Helixi361 – 3633
    Helixi370 – 3734
    Turni377 – 3793
    Helixi380 – 39112
    Beta strandi397 – 4048
    Turni405 – 4073
    Beta strandi408 – 4169

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AFWX-ray1.80A/B25-417[»]
    1AFYmodel-A/B25-417[»]
    1PXTX-ray2.80A/B28-417[»]
    3W15X-ray1.80C1-15[»]
    ProteinModelPortaliP27796.
    SMRiP27796. Positions 25-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27796.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00750000117749.
    HOGENOMiHOG000012239.
    KOiK00632.
    OMAiLYGVESM.
    OrthoDBiEOG7PCJSX.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    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.

    P27796-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQRLQSIKD HLVESAMGKG ESKRKNSLLE KRPEDVVIVA ANRSAIGKGF    50
    KGAFKDVNTD YLLYNFLNEF IGRFPEPLRA DLNLIEEVAC GNVLNVGAGA 100
    TEHRAACLAS GIPYSTPFVA LNRQCSSGLT AVNDIANKIK VGQIDIGLAL 150
    GVESMTNNYK NVNPLGMISS EELQKNREAK KCLIPMGITN ENVAANFKIS 200
    RKDQDEFAAN SYQKAYKAKN EGLFEDEILP IKLPDGSICQ SDEGPRPNVT 250
    AESLSSIRPA FIKDRGTTTA GNASQVSDGV AGVLLARRSV ANQLNLPVLG 300
    RYIDFQTVGV PPEIMGVGPA YAIPKVLEAT GLQVQDIDIF EINEAFAAQA 350
    LYCIHKLGID LNKVNPRGGA IALGHPLGCT GARQVATILR ELKKDQIGVV 400
    SMCIGTGMGA AAIFIKE 417
    Length:417
    Mass (Da):44,730
    Last modified:August 1, 1992 - v1
    Checksum:iB22AA06130829DE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38059 Genomic DNA. Translation: CAA86118.1.
    X53946 Genomic DNA. Translation: CAA37893.1.
    X53395 Genomic DNA. Translation: CAA37472.1.
    AY693184 Genomic DNA. Translation: AAT93203.1.
    BK006942 Genomic DNA. Translation: DAA08392.1.
    PIRiS22784.
    RefSeqiNP_012106.1. NM_001179508.1.

    Genome annotation databases

    EnsemblFungiiYIL160C; YIL160C; YIL160C.
    GeneIDi854646.
    KEGGisce:YIL160C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38059 Genomic DNA. Translation: CAA86118.1 .
    X53946 Genomic DNA. Translation: CAA37893.1 .
    X53395 Genomic DNA. Translation: CAA37472.1 .
    AY693184 Genomic DNA. Translation: AAT93203.1 .
    BK006942 Genomic DNA. Translation: DAA08392.1 .
    PIRi S22784.
    RefSeqi NP_012106.1. NM_001179508.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AFW X-ray 1.80 A/B 25-417 [» ]
    1AFY model - A/B 25-417 [» ]
    1PXT X-ray 2.80 A/B 28-417 [» ]
    3W15 X-ray 1.80 C 1-15 [» ]
    ProteinModelPortali P27796.
    SMRi P27796. Positions 25-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34832. 69 interactions.
    DIPi DIP-1504N.
    IntActi P27796. 3 interactions.
    MINTi MINT-412295.
    STRINGi 4932.YIL160C.

    2D gel databases

    UCD-2DPAGE P27796.

    Proteomic databases

    PaxDbi P27796.
    PeptideAtlasi P27796.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIL160C ; YIL160C ; YIL160C .
    GeneIDi 854646.
    KEGGi sce:YIL160C.

    Organism-specific databases

    CYGDi YIL160c.
    SGDi S000001422. POT1.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00750000117749.
    HOGENOMi HOG000012239.
    KOi K00632.
    OMAi LYGVESM.
    OrthoDBi EOG7PCJSX.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .
    BioCyci MetaCyc:YIL160C-MONOMER.
    YEAST:YIL160C-MONOMER.
    Reactomei REACT_188947. alpha-linolenic acid (ALA) metabolism.

    Miscellaneous databases

    EvolutionaryTracei P27796.
    NextBioi 977187.
    PROi P27796.

    Gene expression databases

    Genevestigatori P27796.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae."
      Einerhand A.W.C., Voorn-Brouwer M.M., Erdmann R., Kunau W.H., Tabak H.F.
      Eur. J. Biochem. 200:113-122(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BJ1991.
    2. "A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus."
      Igual J.C., Matallana E., Gonzalez-Bosch C., Franco L., Perez-Ortin J.E.
      Yeast 7:379-389(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo."
      Glover J.R., Andrews D.W., Subramani S., Rachubinski R.A.
      J. Biol. Chem. 269:7558-7563(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF N-TERMINAL PTS REGION.
    7. "The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology."
      Mathieu M., Zeelen J.P., Pauptit R.A., Erdmann R., Kunau W.-H., Wierenga R.K.
      Structure 2:797-808(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    8. "The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism."
      Mathieu M., Modis Y., Zeelen J.P., Engel C.K., Abagyan R.A., Ahlberg A., Rasmussen B., Lamzin V.S., Kunau W.H., Wierenga R.K.
      J. Mol. Biol. 273:714-728(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiTHIK_YEAST
    AccessioniPrimary (citable) accession number: P27796
    Secondary accession number(s): D6VVC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3