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Protein

Chorismate pyruvate-lyase

Gene

ubiC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.

Catalytic activityi

Chorismate = 4-hydroxybenzoate + pyruvate.

Enzyme regulationi

Inhibited by 4-hydroxybenzoate, vanillate, 4-hydroxybenzaldehyde and 3-carboxymethylaminomethyl-4-hydroxybenzoic acid.2 Publications

Kineticsi

  1. KM=29 µM for chorismate1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Pathway:iubiquinone biosynthesis

    This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351Substrate; via amide nitrogen
    Binding sitei77 – 771Substrate
    Binding sitei115 – 1151Substrate; via amide nitrogen

    GO - Molecular functioni

    • chorismate lyase activity Source: EcoCyc

    GO - Biological processi

    • pyruvate biosynthetic process Source: UniProtKB-HAMAP
    • ubiquinone biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Ubiquinone biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:CHORPYRLY-MONOMER.
    ECOL316407:JW5713-MONOMER.
    MetaCyc:CHORPYRLY-MONOMER.
    BRENDAi4.1.3.40. 2026.
    UniPathwayiUPA00232.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chorismate pyruvate-lyase (EC:4.1.3.40)
    Short name:
    CL
    Short name:
    CPL
    Gene namesi
    Name:ubiC
    Ordered Locus Names:b4039, JW5713
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11369. ubiC.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911G → A: Increases the inhibition by product by about 40%. No effect on substrate affinity. 1 Publication
    Mutagenesisi156 – 1561E → K: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 165164Chorismate pyruvate-lyasePRO_0000065711Add
    BLAST

    Proteomic databases

    PaxDbiP26602.
    PRIDEiP26602.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    aceEP0AFG81EBI-559360,EBI-542683

    Protein-protein interaction databases

    DIPiDIP-11066N.
    IntActiP26602. 3 interactions.
    MINTiMINT-1235748.
    STRINGi511145.b4039.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 118Combined sources
    Beta strandi13 – 175Combined sources
    Helixi23 – 308Combined sources
    Helixi36 – 405Combined sources
    Turni41 – 433Combined sources
    Beta strandi46 – 5611Combined sources
    Helixi58 – 603Combined sources
    Turni62 – 643Combined sources
    Helixi65 – 673Combined sources
    Beta strandi74 – 8310Combined sources
    Beta strandi86 – 9611Combined sources
    Helixi97 – 993Combined sources
    Helixi102 – 1087Combined sources
    Beta strandi111 – 1133Combined sources
    Helixi117 – 1193Combined sources
    Beta strandi121 – 1233Combined sources
    Beta strandi125 – 13511Combined sources
    Beta strandi138 – 14710Combined sources
    Beta strandi150 – 1589Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FW9X-ray1.40A2-165[»]
    1G1BX-ray1.99A/B2-165[»]
    1G81X-ray1.71A2-165[»]
    1JD3X-ray2.03A2-165[»]
    1TT8X-ray1.00A2-165[»]
    1XLRX-ray1.94A2-165[»]
    2AHCX-ray2.40A/B/C/D2-165[»]
    ProteinModelPortaliP26602.
    SMRiP26602. Positions 2-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26602.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UbiC family.Curated

    Phylogenomic databases

    eggNOGiCOG3161.
    HOGENOMiHOG000137785.
    InParanoidiP26602.
    KOiK03181.
    OMAiELWGRRS.
    OrthoDBiEOG6GBM9Z.

    Family and domain databases

    Gene3Di3.40.1410.10. 1 hit.
    HAMAPiMF_01632. UbiC.
    InterProiIPR007440. Chorismate--pyruvate_lyase.
    IPR028978. Chorismate_lyase_/UTRA_dom.
    [Graphical view]
    PfamiPF04345. Chor_lyase. 1 hit.
    [Graphical view]
    SUPFAMiSSF64288. SSF64288. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P26602-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSHPALTQLR ALRYCKEIPA LDPQLLDWLL LEDSMTKRFE QQGKTVSVTM
    60 70 80 90 100
    IREGFVEQNE IPEELPLLPK ESRYWLREIL LCADGEPWLA GRTVVPVSTL
    110 120 130 140 150
    SGPELALQKL GKTPLGRYLF TSSTLTRDFI EIGRDAGLWG RRSRLRLSGK
    160
    PLLLTELFLP ASPLY
    Length:165
    Mass (Da):18,777
    Last modified:January 23, 2007 - v2
    Checksum:i6DAACD25BC338F09
    GO

    Sequence cautioni

    The sequence AAC43133.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence CAA40681.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66619 Genomic DNA. Translation: CAA47181.1.
    M93136 Genomic DNA. Translation: AAA24711.1.
    M93413 Genomic DNA. Translation: AAA24716.1.
    X57434 Genomic DNA. Translation: CAA40681.1. Different initiation.
    M96268 Unassigned DNA. Translation: AAA17027.1.
    DQ087228 Genomic DNA. Translation: AAY88959.1.
    U00006 Genomic DNA. Translation: AAC43133.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77009.2.
    AP009048 Genomic DNA. Translation: BAE78041.1.
    PIRiS25660.
    RefSeqiNP_418463.4. NC_000913.3.
    WP_001326644.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77009; AAC77009; b4039.
    BAE78041; BAE78041; BAE78041.
    GeneIDi948545.
    KEGGiebe:B21_03871.
    ebl:ECD_03911.
    eco:b4039.
    PATRICi32123615. VBIEscCol129921_4156.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66619 Genomic DNA. Translation: CAA47181.1.
    M93136 Genomic DNA. Translation: AAA24711.1.
    M93413 Genomic DNA. Translation: AAA24716.1.
    X57434 Genomic DNA. Translation: CAA40681.1. Different initiation.
    M96268 Unassigned DNA. Translation: AAA17027.1.
    DQ087228 Genomic DNA. Translation: AAY88959.1.
    U00006 Genomic DNA. Translation: AAC43133.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77009.2.
    AP009048 Genomic DNA. Translation: BAE78041.1.
    PIRiS25660.
    RefSeqiNP_418463.4. NC_000913.3.
    WP_001326644.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FW9X-ray1.40A2-165[»]
    1G1BX-ray1.99A/B2-165[»]
    1G81X-ray1.71A2-165[»]
    1JD3X-ray2.03A2-165[»]
    1TT8X-ray1.00A2-165[»]
    1XLRX-ray1.94A2-165[»]
    2AHCX-ray2.40A/B/C/D2-165[»]
    ProteinModelPortaliP26602.
    SMRiP26602. Positions 2-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-11066N.
    IntActiP26602. 3 interactions.
    MINTiMINT-1235748.
    STRINGi511145.b4039.

    Proteomic databases

    PaxDbiP26602.
    PRIDEiP26602.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77009; AAC77009; b4039.
    BAE78041; BAE78041; BAE78041.
    GeneIDi948545.
    KEGGiebe:B21_03871.
    ebl:ECD_03911.
    eco:b4039.
    PATRICi32123615. VBIEscCol129921_4156.

    Organism-specific databases

    EchoBASEiEB1343.
    EcoGeneiEG11369. ubiC.

    Phylogenomic databases

    eggNOGiCOG3161.
    HOGENOMiHOG000137785.
    InParanoidiP26602.
    KOiK03181.
    OMAiELWGRRS.
    OrthoDBiEOG6GBM9Z.

    Enzyme and pathway databases

    UniPathwayiUPA00232.
    BioCyciEcoCyc:CHORPYRLY-MONOMER.
    ECOL316407:JW5713-MONOMER.
    MetaCyc:CHORPYRLY-MONOMER.
    BRENDAi4.1.3.40. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP26602.
    PROiP26602.

    Family and domain databases

    Gene3Di3.40.1410.10. 1 hit.
    HAMAPiMF_01632. UbiC.
    InterProiIPR007440. Chorismate--pyruvate_lyase.
    IPR028978. Chorismate_lyase_/UTRA_dom.
    [Graphical view]
    PfamiPF04345. Chor_lyase. 1 hit.
    [Graphical view]
    SUPFAMiSSF64288. SSF64288. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli."
      Siebert M., Bechthold A., Melzer M., May U., Berger U., Schroeder G., Schroeder J., Severin K., Heide L.
      FEBS Lett. 307:347-350(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    2. "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase."
      Nichols B.P., Green J.M.
      J. Bacteriol. 174:5309-5316(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
      Strain: K12.
    3. "Location of the ubiA gene on the physical map of Escherichia coli."
      Nishimura K., Nakahigashi K., Inokuchi H.
      J. Bacteriol. 174:5762-5762(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase."
      Wu G., Williams H.D., Gibson F., Poole R.K.
      J. Gen. Microbiol. 139:1795-1805(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    5. Zhang D., Shrestha B., Tan T.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BL21.
    6. "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.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "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.
    9. "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase."
      Siebert M., Severin K., Heide L.
      Microbiology 140:897-904(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-156.
    10. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
      Strain: K12 / MG1655 / ATCC 47076.
    11. "Crystallization and 1.1-A diffraction of chorismate lyase from Escherichia coli."
      Stover C., Mayhew M.P., Holden M.J., Howard A., Gallagher D.T.
      J. Struct. Biol. 129:96-99(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
    12. "The crystal structure of chorismate lyase shows a new fold and a tightly retained product."
      Gallagher D.T., Mayhew M., Holden M.J., Howard A., Kim K.-J., Vilker V.L.
      Proteins 44:304-311(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PRODUCT; MUTANT SER-15/SER-82 IN COMPLEX WITH PRODUCT; MUTANT SER-15 IN COMPLEX WITH PRODUCT.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF MUTANT SER-15/SER-82 IN COMPLEXES WITH PRODUCT AND SUBSTRATE ANALOG; MUTANT SER-15/SER-82/ALA-91 IN COMPLEXES WITH PRODUCT AND SUBSTRATE ANALOG, MUTAGENESIS OF GLY-91, ENZYME REGULATION.

    Entry informationi

    Entry nameiUBIC_ECOLI
    AccessioniPrimary (citable) accession number: P26602
    Secondary accession number(s): P76783, Q2M6R5, Q4JHR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 135 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

    3D-structure, Complete proteome, Direct protein sequencing, 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

    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.