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P0A9G6

- ACEA_ECOLI

UniProt

P0A9G6 - ACEA_ECOLI

Protein

Isocitrate lyase

Gene

aceA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway By similarity.By similarity

    Catalytic activityi

    Isocitrate = succinate + glyoxylate.PROSITE-ProRule annotation

    Cofactori

    Divalent cations.

    Enzyme regulationi

    Is activated by phosphorylation (on histidine) and is inhibited by PEP, 3-phosphoglycerate and succinate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei195 – 1951Curated

    GO - Molecular functioni

    1. cation binding Source: EcoliWiki
    2. isocitrate lyase activity Source: EcoliWiki

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciEcoCyc:ISOCIT-LYASE-MONOMER.
    ECOL316407:JW3975-MONOMER.
    MetaCyc:ISOCIT-LYASE-MONOMER.
    UniPathwayiUPA00703; UER00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate lyase (EC:4.1.3.1)
    Short name:
    ICL
    Short name:
    Isocitrase
    Short name:
    Isocitratase
    Gene namesi
    Name:aceA
    Synonyms:icl
    Ordered Locus Names:b4015, JW3975
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10022. aceA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi195 – 1951C → A: Large decrease in activity. 1 Publication
    Mutagenesisi195 – 1951C → S: Large decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Isocitrate lyasePRO_0000068774Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0A9G6.
    PRIDEiP0A9G6.

    2D gel databases

    SWISS-2DPAGEP0A9G6.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9G6.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    DIPiDIP-35893N.
    IntActiP0A9G6. 3 interactions.
    STRINGi511145.b4015.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1411
    Helixi18 – 203
    Helixi29 – 346
    Helixi44 – 5714
    Turni58 – 603
    Beta strandi61 – 7010
    Helixi74 – 8310
    Beta strandi88 – 903
    Helixi92 – 987
    Beta strandi108 – 1103
    Helixi116 – 13722
    Beta strandi154 – 1574
    Beta strandi162 – 1643
    Helixi165 – 17713
    Beta strandi181 – 1888
    Helixi190 – 1923
    Helixi206 – 22318
    Beta strandi228 – 2336
    Turni235 – 2373
    Beta strandi240 – 2423
    Helixi247 – 2526
    Beta strandi253 – 2575
    Beta strandi263 – 2653
    Helixi269 – 27911
    Helixi280 – 2823
    Beta strandi284 – 2885
    Helixi295 – 30814
    Beta strandi313 – 3175
    Helixi336 – 3438
    Beta strandi345 – 3506
    Helixi353 – 37119
    Helixi374 – 3818
    Helixi383 – 3908
    Turni391 – 3933
    Helixi399 – 4024
    Helixi405 – 41511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IGWX-ray2.10A/B/C/D1-434[»]
    ProteinModelPortaliP0A9G6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9G6.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2224.
    HOGENOMiHOG000238475.
    KOiK01637.
    OMAiDQIQWAN.
    OrthoDBiEOG689HMX.
    PhylomeDBiP0A9G6.

    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. 2 hits.
    [Graphical view]
    PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
    PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9G6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA    50
    AKMWRLLHGE SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN 100
    LAASMYPDQS LYPANSVPAV VERINNTFRR ADQIQWSAGI EPGDPRYVDY 150
    FLPIVADAEA GFGGVLNAFE LMKAMIEAGA AAVHFEDQLA SVKKCGHMGG 200
    KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL ITSDCDPYDS 250
    EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR 300
    FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI 350
    TLAGIHSMWF NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ 400
    QEVGTGYFDK VTTIIQGGTS SVTALTGSTE ESQF 434
    Length:434
    Mass (Da):47,522
    Last modified:July 19, 2005 - v1
    Checksum:iF66449CCD1E168E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 11717LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416. (PubMed:3290857)CuratedAdd
    BLAST
    Sequence conflicti215 – 2151A → P in CAA30416. (PubMed:3290857)Curated
    Sequence conflicti293 – 2931P → R in AAA24009. (PubMed:2836370)Curated
    Sequence conflicti338 – 3381Q → E in CAA30416. (PubMed:3290857)Curated
    Sequence conflicti419 – 43416TSSVT…EESQF → DVFSHRADRLH(PubMed:3049537)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12431 Genomic DNA. Translation: CAA30974.1.
    X07543 Genomic DNA. Translation: CAA30416.1.
    M22621 Genomic DNA. Translation: AAC13650.1.
    U00006 Genomic DNA. Translation: AAC43109.1.
    U00096 Genomic DNA. Translation: AAC76985.1.
    AP009048 Genomic DNA. Translation: BAE78017.1.
    M20714 Genomic DNA. Translation: AAA24009.1.
    PIRiS05692. WZECIC.
    RefSeqiNP_418439.1. NC_000913.3.
    YP_492158.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76985; AAC76985; b4015.
    BAE78017; BAE78017; BAE78017.
    GeneIDi12934475.
    948517.
    KEGGiecj:Y75_p3902.
    eco:b4015.
    PATRICi32123557. VBIEscCol129921_4127.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12431 Genomic DNA. Translation: CAA30974.1 .
    X07543 Genomic DNA. Translation: CAA30416.1 .
    M22621 Genomic DNA. Translation: AAC13650.1 .
    U00006 Genomic DNA. Translation: AAC43109.1 .
    U00096 Genomic DNA. Translation: AAC76985.1 .
    AP009048 Genomic DNA. Translation: BAE78017.1 .
    M20714 Genomic DNA. Translation: AAA24009.1 .
    PIRi S05692. WZECIC.
    RefSeqi NP_418439.1. NC_000913.3.
    YP_492158.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IGW X-ray 2.10 A/B/C/D 1-434 [» ]
    ProteinModelPortali P0A9G6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35893N.
    IntActi P0A9G6. 3 interactions.
    STRINGi 511145.b4015.

    2D gel databases

    SWISS-2DPAGE P0A9G6.

    Proteomic databases

    PaxDbi P0A9G6.
    PRIDEi P0A9G6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76985 ; AAC76985 ; b4015 .
    BAE78017 ; BAE78017 ; BAE78017 .
    GeneIDi 12934475.
    948517.
    KEGGi ecj:Y75_p3902.
    eco:b4015.
    PATRICi 32123557. VBIEscCol129921_4127.

    Organism-specific databases

    EchoBASEi EB0021.
    EcoGenei EG10022. aceA.

    Phylogenomic databases

    eggNOGi COG2224.
    HOGENOMi HOG000238475.
    KOi K01637.
    OMAi DQIQWAN.
    OrthoDBi EOG689HMX.
    PhylomeDBi P0A9G6.

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00719 .
    BioCyci EcoCyc:ISOCIT-LYASE-MONOMER.
    ECOL316407:JW3975-MONOMER.
    MetaCyc:ISOCIT-LYASE-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9G6.
    PROi P0A9G6.

    Gene expression databases

    Genevestigatori P0A9G6.

    Family and domain databases

    Gene3Di 3.20.20.60. 1 hit.
    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. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMi SSF51621. SSF51621. 1 hit.
    TIGRFAMsi TIGR01346. isocit_lyase. 2 hits.
    PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
      Byrne C.R., Stokes H.W., Ward K.A.
      Nucleic Acids Res. 16:9342-9342(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
      Byrne C.R., Stokes H.W., Ward K.A.
      Nucleic Acids Res. 16:10924-10924(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Nucleotide sequence of the aceA gene coding for isocitrate lyase in Escherichia coli."
      Rieul C., Bleicher F., Duclos B., Cortay J.-C., Cozzone A.J.
      Nucleic Acids Res. 16:5689-5689(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."
      Matsuoka M., McFadden B.A.
      J. Bacteriol. 170:4528-4536(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase."
      Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., Laporte D.C.
      J. Bacteriol. 170:2763-2769(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-434.
    9. "Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli."
      Robertson E.F., Hoyt J.C., Reeves H.C.
      J. Biol. Chem. 263:2477-2482(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    10. "Escherichia coli isocitrate lyase: properties and comparisons."
      Hoyt J.C., Robertson E.F., Berlyn K.A., Reeves H.C.
      Biochim. Biophys. Acta 966:30-35(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308."
      Robertson A.G., Nimmo H.G.
      Biochem. J. 305:239-244(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-195.
      Strain: ML308.

    Entry informationi

    Entry nameiACEA_ECOLI
    AccessioniPrimary (citable) accession number: P0A9G6
    Secondary accession number(s): P05313, Q2M6T9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3