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P28240

- ACEA_YEAST

UniProt

P28240 - ACEA_YEAST

Protein

Isocitrate lyase

Gene

ICL1

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 128 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.

    Catalytic activityi

    Isocitrate = succinate + glyoxylate.PROSITE-ProRule annotation

    Enzyme regulationi

    Phosphorylated and inactivated after addition of glucose to the cell culture (repressing conditions).

    Kineticsi

    The Vmax with threo-D(S)-isocitrate as substrate is 5-fold higher than with threo-D(S)-2-methylisocitrate as substrate.

    1. KM=1.4 mM for threo-D(S)-isocitrate (at pH 7.0)2 Publications
    2. KM=0.6 mM for threo-D(S)-2-methylisocitrate (at pH 7.0 and 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 7.2 Publications

    Temperature dependencei

    Thermostable for 60 minutes up to 50 degrees Celsius.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei217 – 2171Curated

    GO - Molecular functioni

    1. isocitrate lyase activity Source: SGD

    GO - Biological processi

    1. glyoxylate cycle Source: SGD
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciYEAST:YER065C-MONOMER.
    SABIO-RKP28240.
    UniPathwayiUPA00703; UER00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate lyase (EC:4.1.3.1)
    Short name:
    ICL
    Alternative name(s):
    Threo-D(S)-isocitrate glyoxylate-lyase
    Short name:
    Isocitrase
    Short name:
    Isocitratase
    Gene namesi
    Name:ICL1
    Ordered Locus Names:YER065C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER065c.
    SGDiS000000867. ICL1.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531T → A: Abolishes short-term enzyme inactivation by glucose addition. 1 Publication
    Mutagenesisi216 – 2161K → R: Reduces activity by 45%; when associated with L-220. 1 Publication
    Mutagenesisi220 – 2201M → L: Reduces activity by 45%; when associated with R-216. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 557557Isocitrate lyasePRO_0000068799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531PhosphothreonineSequence Analysis

    Post-translational modificationi

    Phosphorylated in response to elevated glucose levels, leading first to reversible inactivation of the enzyme (short-term inactivation), and at a later stage to proteolytic degradation of the protein (long-term inactivation).1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP28240.
    PaxDbiP28240.
    PeptideAtlasiP28240.

    Expressioni

    Inductioni

    Repressed by glucose and induced by ethanol via the transcriptional activator CAT8.3 Publications

    Gene expression databases

    GenevestigatoriP28240.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi36807. 29 interactions.
    DIPiDIP-1663N.
    IntActiP28240. 2 interactions.
    MINTiMINT-400647.
    STRINGi4932.YER065C.

    Structurei

    3D structure databases

    ProteinModelPortaliP28240.
    SMRiP28240. Positions 22-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2224.
    GeneTreeiENSGT00510000053163.
    HOGENOMiHOG000238475.
    KOiK01637.
    OMAiALISHQF.
    OrthoDBiEOG73Z331.

    Family and domain databases

    Gene3Di3.20.20.60. 2 hits.
    InterProiIPR006254. Isocitrate_lyase.
    IPR018523. Isocitrate_lyase_ph_CS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
    PfamiPF00463. ICL. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
    PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28240-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIPVGNTKN DFAALQAKLD ADAAEIEKWW SDSRWSKTKR NYSARDIAVR    50
    RGTFPPIEYP SSVMARKLFK VLEKHHNEGT VSKTFGALDP VQISQMAKYL 100
    DTIYISGWQC SSTASTSNEP GPDLADYPMD TVPNKVEHLF KAQLFHDRKQ 150
    LEARSKAKSQ EELDEMGAPI DYLTPIVADA DAGHGGLTAV FKLTKMFIER 200
    GAAGIHMEDQ TSTNKKCGHM AGRCVIPVQE HVNRLVTIRM CADIMHSDLI 250
    VVARTDSEAA TLISSTIDTR DHYFIVGATN PNIEPFAEVL NDAIMSGASG 300
    QELADIEQKW CRDAGLKLFH EAVIDEIERS ALSNKQELIK KFTSKVGPLT 350
    ETSHREAKKL AKEILGHEIF FDWELPRVRE GLYRYRGGTQ CSIMRARAFA 400
    PYADLVWMES NYPDFQQAKE FAEGVKEKFP DQWLAYNLSP SFNWPKAMSV 450
    DEQHTFIQRL GDLGYIWQFI TLAGLHTNAL AVHNFSRDFA KDGMKAYAQN 500
    VQQREMDDGV DVLKHQKWSG AEYIDGLLKL AQGGVSATAA MGTGVTEDQF 550
    KENGVKK 557
    Length:557
    Mass (Da):62,409
    Last modified:December 1, 1992 - v1
    Checksum:i15CC5A169CCEBE8B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61271 Genomic DNA. Translation: CAA43575.1.
    X65554 Genomic DNA. Translation: CAA46523.1.
    U18813 Genomic DNA. Translation: AAB64601.1.
    BK006939 Genomic DNA. Translation: DAA07724.1.
    PIRiS22386. WZBYI.
    RefSeqiNP_010987.3. NM_001178956.3.

    Genome annotation databases

    EnsemblFungiiYER065C; YER065C; YER065C.
    GeneIDi856794.
    KEGGisce:YER065C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61271 Genomic DNA. Translation: CAA43575.1 .
    X65554 Genomic DNA. Translation: CAA46523.1 .
    U18813 Genomic DNA. Translation: AAB64601.1 .
    BK006939 Genomic DNA. Translation: DAA07724.1 .
    PIRi S22386. WZBYI.
    RefSeqi NP_010987.3. NM_001178956.3.

    3D structure databases

    ProteinModelPortali P28240.
    SMRi P28240. Positions 22-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36807. 29 interactions.
    DIPi DIP-1663N.
    IntActi P28240. 2 interactions.
    MINTi MINT-400647.
    STRINGi 4932.YER065C.

    Proteomic databases

    MaxQBi P28240.
    PaxDbi P28240.
    PeptideAtlasi P28240.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER065C ; YER065C ; YER065C .
    GeneIDi 856794.
    KEGGi sce:YER065C.

    Organism-specific databases

    CYGDi YER065c.
    SGDi S000000867. ICL1.

    Phylogenomic databases

    eggNOGi COG2224.
    GeneTreei ENSGT00510000053163.
    HOGENOMi HOG000238475.
    KOi K01637.
    OMAi ALISHQF.
    OrthoDBi EOG73Z331.

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00719 .
    BioCyci YEAST:YER065C-MONOMER.
    SABIO-RK P28240.

    Miscellaneous databases

    NextBioi 983030.

    Gene expression databases

    Genevestigatori P28240.

    Family and domain databases

    Gene3Di 3.20.20.60. 2 hits.
    InterProi IPR006254. Isocitrate_lyase.
    IPR018523. Isocitrate_lyase_ph_CS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
    Pfami PF00463. ICL. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR01346. isocit_lyase. 1 hit.
    PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structure and regulation of the isocitrate lyase gene ICL1 from the yeast Saccharomyces cerevisiae."
      Schoeler A., Schueller H.-J.
      Curr. Genet. 23:375-381(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: DBY939.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Production of pyruvate and succinate by action of isocitrate lyase on alpha-methylisocitrate."
      McFadden B.A., Rose I.A., Williams J.O.
      Arch. Biochem. Biophys. 148:84-88(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Glucose-stimulated phosphorylation of yeast isocitrate lyase in vivo."
      Lopez-Boado Y.S., Herrero P., Fernandez M.-T., Fernandez R., Moreno F.
      J. Gen. Microbiol. 134:2499-2505(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INDUCTION.
    7. "Purification of isocitrate lyase from Saccharomyces cerevisiae."
      Lopez-Boado Y.S., Herrero P., Fernandez M.-T., Fernandez R., Moreno F.
      Yeast 4:41-46(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    8. "Localization and targeting of isocitrate lyases in Saccharomyces cerevisiae."
      Taylor K.M., Kaplan C.P., Gao X., Baker A.
      Biochem. J. 319:255-262(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Glucose-induced inactivation of isocitrate lyase in Saccharomyces cerevisiae is mediated by the cAMP-dependent protein kinase catalytic subunits Tpk1 and Tpk2."
      Ordiz I., Herrero P., Rodicio R., Moreno F.
      FEBS Lett. 385:43-46(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-53.
    10. "Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in Saccharomyces cerevisiae."
      Heinisch J.J., Valdes E., Alvarez J., Rodicio R.
      Yeast 12:1285-1295(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-216 AND MET-220.
    11. "Isocitrate lyase localisation in Saccharomyces cerevisiae cells."
      Chaves R.S., Herrero P., Ordiz I., Angeles del Brio M., Moreno F.
      Gene 198:165-169(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Deregulation of gluconeogenic structural genes by variants of the transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae."
      Rahner A., Hiesinger M., Schueller H.-J.
      Mol. Microbiol. 34:146-156(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiACEA_YEAST
    AccessioniPrimary (citable) accession number: P28240
    Secondary accession number(s): D3DLX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Yeast isocitrate lyase is the only eukaryotic member of this family that is located in the cytoplasm, instead of being targeted to the peroxisome or the glyoxysome.
    The Pseudomonas indigofera ortholog enzyme can be inactivated by beta-bromopyruvate.

    Keywords - Technical termi

    Complete proteome, 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3