Summary: Chorismate lyase
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Chorismate lyase Edit Wikipedia article
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| Chorismate lyase | |||||||
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| Identifiers | |||||||
| EC number | 4.1.3.40 | ||||||
| CAS number | 157482-18-3 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
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| chorismate lyase with product, 1.0 a resolution | |||||||||
| Identifiers | |||||||||
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| Symbol | Chor_lyase | ||||||||
| Pfam | PF04345 | ||||||||
| Pfam clan | CL0122 | ||||||||
| InterPro | IPR007440 | ||||||||
| SCOP | 1jd3 | ||||||||
| SUPERFAMILY | 1jd3 | ||||||||
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In enzymology, a chorismate lyase (EC 4.1.3.40) is an enzyme that catalyzes the chemical reaction
- chorismate
4-hydroxybenzoate + pyruvate
Hence, this enzyme has one substrate, chorismate, and two products, 4-hydroxybenzoate and pyruvate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). Other names in common use include CL, CPL, and UbiC.
This enzyme catalyses the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria.[1] Its activity does not require metal cofactors.[2]
[edit] References
- ^ Nichols BP, Green JM (August 1992). "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase". J. Bacteriol. 174 (16): 5309–16. PMC 206367. PMID 1644758. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=206367.
- ^ Siebert M, Severin K, Heide L (April 1994). "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase". Microbiology (Reading, Engl.) 140 (4): 897–904. doi:10.1099/00221287-140-4-897. PMID 8012607.
[edit] Further reading
- Nichols BP, Green JM (1992). "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase". J. Bacteriol. 174 (16): 5309–16. PMC 206367. PMID 1644758. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=206367.
- Siebert M, Severin K, Heide L (Pt 4). "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase". Microbiology. 140 (4): 897–904. doi:10.1099/00221287-140-4-897. PMID 8012607.
- Meganathan R (2001). "Ubiquinone biosynthesis in microorganisms". FEMS. Microbiol. Lett. 203 (2): 131–9. doi:10.1111/j.1574-6968.2001.tb10831.x. PMID 11583838.
This article incorporates text from the public domain Pfam and InterPro IPR007440
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Chorismate lyase Provide feedback
Chorismate lyase catalyses the first step in ubiquinone synthesis, i.e. the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate.
Literature references
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Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL; , Proteins 2001;44:304-311.: The crystal structure of chorismate lyase shows a new fold and a tightly retained product. PUBMED:11455603 EPMC:11455603
External database links
| PANDIT: | PF04345 |
| Pseudofam: | PF04345 |
| SCOP: | 1jd3 |
| SYSTERS: | Chor_lyase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007440
Chorismate--pyruvate lyase catalyses the first step in ubiquinone synthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria [PUBMED:1644758]. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine [PUBMED:11583838], however this enzyme is found only in bacteria. Its activity does not require metal cofactors [PUBMED:8012607].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | chorismate lyase activity (GO:0008813) |
| Biological process | ubiquinone biosynthetic process (GO:0006744) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
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| Seed (3) |
Full (1188) |
Representative proteomes | NCBI (690) |
Meta (245) |
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| RP15 (34) |
RP35 (86) |
RP55 (143) |
RP75 (198) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (3) |
Full (1188) |
Representative proteomes | NCBI (690) |
Meta (245) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (34) |
RP35 (86) |
RP55 (143) |
RP75 (198) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | COG3161 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Mifsud W |
| Number in seed: | 3 |
| Number in full: | 1188 |
| Average length of the domain: | 159.80 aa |
| Average identity of full alignment: | 37 % |
| Average coverage of the sequence by the domain: | 92.75 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 168 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Chor_lyaseStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Chor_lyase domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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4-hydroxybenzoate + pyruvate
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence