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P26602 (UBIC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chorismate pyruvate-lyase

Short name=CL
Short name=CPL
EC=4.1.3.40
Gene names
Name:ubiC
Ordered Locus Names:b4039, JW5713
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. HAMAP-Rule MF_01632

Catalytic activity

Chorismate = 4-hydroxybenzoate + pyruvate. HAMAP-Rule MF_01632

Enzyme regulation

Inhibited by 4-hydroxybenzoate, vanillate, 4-hydroxybenzaldehyde and 3-carboxymethylaminomethyl-4-hydroxybenzoic acid. Ref.10 Ref.13

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis. HAMAP-Rule MF_01632

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_01632.

Sequence similarities

Belongs to the UbiC family.

Biophysicochemical properties

Kinetic parameters:

KM=29 µM for chorismate Ref.10

pH dependence:

Optimum pH is 7.5.

Sequence caution

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

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

Ontologies

Keywords
   Biological processUbiquinone biosynthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpyruvate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ubiquinone biosynthetic process

Inferred from mutant phenotype PubMed 4595202. Source: EcoCyc

   Cellular_componentcytosol

Inferred from direct assay Ref.2. Source: EcoCyc

   Molecular_functionchorismate lyase activity

Inferred from direct assay Ref.2. Source: EcoCyc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceEP0AFG81EBI-559360,EBI-542683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 165164Chorismate pyruvate-lyase HAMAP-Rule MF_01632
PRO_0000065711

Sites

Binding site351Substrate; via amide nitrogen
Binding site771Substrate
Binding site1151Substrate; via amide nitrogen

Experimental info

Mutagenesis911G → A: Increases the inhibition by product by about 40%. No effect on substrate affinity. Ref.13
Mutagenesis1561E → K: Loss of activity. Ref.9

Secondary structure

.................................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26602 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6DAACD25BC338F09

FASTA16518,777
        10         20         30         40         50         60 
MSHPALTQLR ALRYCKEIPA LDPQLLDWLL LEDSMTKRFE QQGKTVSVTM IREGFVEQNE 

        70         80         90        100        110        120 
IPEELPLLPK ESRYWLREIL LCADGEPWLA GRTVVPVSTL SGPELALQKL GKTPLGRYLF 

       130        140        150        160 
TSSTLTRDFI EIGRDAGLWG RRSRLRLSGK PLLLTELFLP ASPLY 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Chorismate lyase: kinetics and engineering for stability."
Holden M.J., Mayhew M.P., Gallagher D.T., Vilker V.L.
Biochim. Biophys. Acta 1594:160-167(2002) [PubMed] [Europe PMC] [Abstract]
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]"Structural analysis of ligand binding and catalysis in chorismate lyase."
Smith N., Roitberg A.E., Rivera E., Howard A., Holden M.J., Mayhew M., Kaistha S., Gallagher D.T.
Arch. Biochem. Biophys. 445:72-80(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS25660.
RefSeqNP_418463.4. NC_000913.3.
YP_492182.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP26602.
SMRP26602. Positions 2-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11066N.
IntActP26602. 3 interactions.
MINTMINT-1235748.
STRING511145.b4039.

Proteomic databases

PaxDbP26602.
PRIDEP26602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77009; AAC77009; b4039.
BAE78041; BAE78041; BAE78041.
GeneID12933664.
948545.
KEGGecj:Y75_p3926.
eco:b4039.
PATRIC32123615. VBIEscCol129921_4156.

Organism-specific databases

EchoBASEEB1343.
EcoGeneEG11369. ubiC.

Phylogenomic databases

eggNOGCOG3161.
HOGENOMHOG000137785.
KOK03181.
OMARTVIPQE.
OrthoDBEOG6GBM9Z.
ProtClustDBPRK11655.

Enzyme and pathway databases

BioCycEcoCyc:CHORPYRLY-MONOMER.
ECOL316407:JW5713-MONOMER.
MetaCyc:CHORPYRLY-MONOMER.
BRENDA4.1.3.40. 2026.
UniPathwayUPA00232.

Gene expression databases

GenevestigatorP26602.

Family and domain databases

HAMAPMF_01632. UbiC.
InterProIPR007440. Chorismate--pyruvate_lyase.
[Graphical view]
PfamPF04345. Chor_lyase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26602.
PROP26602.

Entry information

Entry nameUBIC_ECOLI
AccessionPrimary (citable) accession number: P26602
Secondary accession number(s): P76783, Q2M6R5, Q4JHR8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene