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Protein

Isocitrate lyase

Gene

aceA

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible 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 during growth on fatty acid substrates.1 Publication

Catalytic activityi

Isocitrate = succinate + glyoxylate.1 Publication

Cofactori

Mg2+1 PublicationNote: Divalent metal cations. Mn(2+) or Co2+ can be used.1 Publication

Enzyme regulationi

Inhibited by 3-phosphoglycerate, 6-phosphogluconate, phosphoenolpyruvate (PEP), fructose 1,6-bisphosphate, glycolate, oxalate, and itaconate.1 Publication

Kineticsi

  1. KM=0.28 mM for threo-D-isocitrate.1 Publication
  2. KM=0.34 mM for glyoxylate.1 Publication
  3. KM=0.61 mM for succinate.1 Publication

    pH dependencei

    Optimum pH is 7.3.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius. Above 45 degrees Celsius, the enzyme is denaturated.1 Publication

    Pathway:iglyoxylate cycle

    This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from isocitrate.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Isocitrate lyase (aceA)
    2. Malate synthase G (glcB)
    This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi155 – 1551MagnesiumBy similarity
    Active sitei193 – 1931Proton acceptorBy similarity
    Binding sitei230 – 2301SubstrateBy similarity
    Binding sitei349 – 3491SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Cobalt, Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00703; UER00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate lyase1 Publication (EC:4.1.3.11 Publication)
    Short name:
    ICL1 Publication
    Alternative name(s):
    Isocitrase1 Publication
    Isocitratase1 Publication
    Gene namesi
    Name:aceA1 Publication
    Ordered Locus Names:Cgl2331, cg2560
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to grow on acetate as carbon source.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 432431Isocitrate lyasePRO_0000068773Add
    BLAST

    Expressioni

    Inductioni

    Activated by RamA and repressed by RamB.2 Publications

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-2898N.
    STRINGi196627.cg2560.

    Structurei

    3D structure databases

    ProteinModelPortaliP42449.
    SMRiP42449. Positions 2-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 953Substrate bindingBy similarity
    Regioni194 – 1952Substrate bindingBy similarity
    Regioni315 – 3195Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2224.
    HOGENOMiHOG000238475.
    KOiK01637.
    OMAiLEKDWAE.
    OrthoDBiEOG689HMX.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    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]
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
    PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42449-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNVGKPRTA QEIQQDWDTN PRWNGITRDY TADQVADLQG SVIEEHTLAR
    60 70 80 90 100
    RGSEILWDAV TQEGDGYINA LGALTGNQAV QQVRAGLKAV YLSGWQVAGD
    110 120 130 140 150
    ANLSGHTYPD QSLYPANSVP SVVRRINNAL LRSDEIARTE GDTSVDNWVV
    160 170 180 190 200
    PIVADGEAGF GGALNVYELQ KAMIAAGAAG THWEDQLASE KKCGHLGGKV
    210 220 230 240 250
    LIPTQQHIRT LNSARLAADV ANTPTVVIAR TDAEAATLIT SDVDERDQPF
    260 270 280 290 300
    ITGERTAEGY YHVKNGLEPC IARAKSYAPY ADMIWMETGT PDLELAKKFA
    310 320 330 340 350
    EGVRSEFPDQ LLSYNCSPSF NWSAHLEADE IAKFQKELGA MGFKFQFITL
    360 370 380 390 400
    AGFHSLNYGM FDLAYGYARE GMTSFVDLQN REFKAAEERG FTAVKHQREV
    410 420 430
    GAGYFDQIAT TVDPNSSTTA LKGSTEEGQF HN
    Length:432
    Mass (Da):47,228
    Last modified:January 23, 2007 - v2
    Checksum:iF8B50DA176D32E87
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75504 Genomic DNA. Translation: CAA53219.1.
    BA000036 Genomic DNA. Translation: BAB99724.1.
    BX927154 Genomic DNA. Translation: CAF20674.1.
    PIRiI40713.
    RefSeqiNP_601531.1. NC_003450.3.
    WP_003859378.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB99724; BAB99724; BAB99724.
    CAF20674; CAF20674; cg2560.
    GeneIDi1020281.
    KEGGicgb:cg2560.
    cgl:NCgl2248.
    PATRICi21496664. VBICorGlu203724_2264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75504 Genomic DNA. Translation: CAA53219.1.
    BA000036 Genomic DNA. Translation: BAB99724.1.
    BX927154 Genomic DNA. Translation: CAF20674.1.
    PIRiI40713.
    RefSeqiNP_601531.1. NC_003450.3.
    WP_003859378.1. NC_006958.1.

    3D structure databases

    ProteinModelPortaliP42449.
    SMRiP42449. Positions 2-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-2898N.
    STRINGi196627.cg2560.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB99724; BAB99724; BAB99724.
    CAF20674; CAF20674; cg2560.
    GeneIDi1020281.
    KEGGicgb:cg2560.
    cgl:NCgl2248.
    PATRICi21496664. VBICorGlu203724_2264.

    Phylogenomic databases

    eggNOGiCOG2224.
    HOGENOMiHOG000238475.
    KOiK01637.
    OMAiLEKDWAE.
    OrthoDBiEOG689HMX.

    Enzyme and pathway databases

    UniPathwayiUPA00703; UER00719.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    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]
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
    PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of the isocitrate lyase gene from Corynebacterium glutamicum and biochemical analysis of the enzyme."
      Reinscheid D.J., Eikmanns B.J., Sahm H.
      J. Bacteriol. 176:3474-3483(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    4. "RamB, a novel transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum."
      Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.
      J. Bacteriol. 186:2798-2809(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    5. "Identification of RamA, a novel LuxR-type transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum."
      Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.
      J. Bacteriol. 188:2554-2567(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiACEA_CORGL
    AccessioniPrimary (citable) accession number: P42449
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3

    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 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.