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UniProtKB/Swiss-Prot entry P26602


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBIC_ECOLI
Primary accession number P26602
Secondary accession numbers P76783 Q2M6R5 Q4JHR8
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name Chorismate--pyruvate lyase
Synonyms CL
CPL
EC 4.1.3.40
Gene name
Name: ubiC
OrderedLocusNames: b4039, JW5713
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1016/0014-5793(92)80710-X; PubMed=1644192 [NCBI, ExPASy, EBI, Israel, Japan]
Siebert M., Bechthold A., Melzer M., May U., Berger U., Schroeder G., Schroeder J., Severin K., Heide L.;
"Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli.";
FEBS Lett. 307:347-350(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
STRAIN=K12;
PubMed=1644758 [NCBI, ExPASy, EBI, Israel, Japan]
Nichols B.P., Green J.M.;
"Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase.";
J. Bacteriol. 174:5309-5316(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=1512213 [NCBI, ExPASy, EBI, Israel, Japan]
Nishimura K., Nakahigashi K., Inokuchi H.;
"Location of the ubiA gene on the physical map of Escherichia coli.";
J. Bacteriol. 174:5762-5762(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8409922 [NCBI, ExPASy, EBI, Israel, Japan]
Wu G., Williams H.D., Gibson F., Poole R.K.;
"Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase.";
J. Gen. Microbiol. 139:1795-1805(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BL21;
Zhang D., Shrestha B., Tan T.;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[9]
CHARACTERIZATION, AND MUTAGENESIS OF GLU-156.
PubMed=8012607 [NCBI, ExPASy, EBI, Israel, Japan]
Siebert M., Severin K., Heide L.;
"Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase.";
Microbiology 140:897-904(1994).
[10]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1016/S0167-4838(01)00302-8; PubMed=11825618 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.J., Mayhew M.P., Gallagher D.T., Vilker V.L.;
"Chorismate lyase: kinetics and engineering for stability.";
Biochim. Biophys. Acta 1594:160-167(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
DOI=10.1006/jsbi.1999.4205; PubMed=10675300 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C., Mayhew M.P., Holden M.J., Howard A., Gallagher D.T.;
"Crystallization and 1.1-A diffraction of chorismate lyase from Escherichia coli.";
J. Struct. Biol. 129:96-99(2000).
[12]
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.
DOI=10.1002/prot.1095; PubMed=11455603 [NCBI, ExPASy, EBI, Israel, Japan]
Gallagher D.T., Mayhew M., Holden M.J., Howard A., Kim K.-J., Vilker V.L.;
"The crystal structure of chorismate lyase shows a new fold and a tightly retained product.";
Proteins 44:304-311(2001).
[13]
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, AND ENZYME REGULATION.
DOI=10.1016/j.abb.2005.10.026; PubMed=16343413 [NCBI, ExPASy, EBI, Israel, Japan]
Smith N., Roitberg A.E., Rivera E., Howard A., Holden M.J., Mayhew M., Kaistha S., Gallagher D.T.;
"Structural analysis of ligand binding and catalysis in chorismate lyase.";
Arch. Biochem. Biophys. 445:72-80(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X66619; CAA47181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M93136; AAA24711.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M93413; AAA24716.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57434; CAA40681.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M96268; AAA17027.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ087228; AAY88959.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43133.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77009.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78041.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S25660; S25660.
RefSeq AP_004540.1; -.
NP_418463.4; -.
3D structure databases
PDB
1FW9; X-ray; 1.40 A; A=1-165.[ExPASy / RCSB / EBI]
1G1B; X-ray; 1.99 A; A/B=1-165.[ExPASy / RCSB / EBI]
1G81; X-ray; 1.71 A; A=1-165.[ExPASy / RCSB / EBI]
1JD3; X-ray; 2.03 A; A=1-165.[ExPASy / RCSB / EBI]
1TT8; X-ray; 1.00 A; A=1-165.[ExPASy / RCSB / EBI]
1XLR; X-ray; 1.94 A; A=1-165.[ExPASy / RCSB / EBI]
2AHC; X-ray; 2.40 A; A/B/C/D=1-165.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FW9; -.
1G1B; -.
1G81; -.
1JD3; -.
1TT8; -.
1XLR; -.
2AHC; -.
ModBase P26602.
Protein-protein interaction databases
DIP DIP:11066N; -.
IntAct P26602; -.
Enzyme and pathway databases
BioCyc EcoCyc:CHORPYRLY-MON; -.
MetaCyc:CHORPYRLY-MON; -.
Organism-specific databases
EchoBASE EB1343; -.
EcoGene EG11369; ubiC.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008813; Molecular function: chorismate lyase activity (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0042866; Biological process: pyruvate biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006744; Biological process: ubiquinone biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01632; -; 1.
PBIL [Tree]
InterPro IPR007440; Chor_lyase.
Graphical view of domain structure.
Pfam PF04345; Chor_lyase; 1.
Pfam graphical view of domain structure.
ProtoNet P26602.
Genome annotation databases
GeneID 948545; -.
GenomeReviews U00096_GR; b4039.
AP009048_GR; JW5713.
KEGG ecj:JW5713; -.
eco:b4039; -.
Phylogenomic databases
HOGENOM P26602; -.
Genome annotation databases
CMR P26602; b4039.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Lyase; Ubiquinone biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   165  164     Chorismate--pyruvate lyase. PRO_0000065711
BINDING   35    35        Substrate; via amide nitrogen. 
BINDING   77    77        Substrate. 
BINDING   115   115        Substrate; via amide nitrogen. 
MUTAGEN   91    91        G->A: Increases the inhibition by product by about 40%. No effect on substrate affinity. 
MUTAGEN   156   156        E->K: Loss of activity. 
HELIX   4    11  8      
HELIX   23    30  8      
HELIX   36    40  5      
TURN   41    43  3      
STRAND   46    56  11      
HELIX   58    60  3      
TURN   62    64  3      
HELIX   65    67  3      
STRAND   74    83  10      
STRAND   86    96  11      
HELIX   97    99  3      
HELIX   102   108  7      
HELIX   117   119  3      
STRAND   125   135  11      
STRAND   138   147  10      
STRAND   150   158  9      
Sequence information
Length: 165 AA [This is the length of the unprocessed precursor] Molecular weight: 18777 Da [This is the MW of the unprocessed precursor] CRC64: 6DAACD25BC338F09 [This is a checksum on the sequence]
        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 

P26602 in FASTA format

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