Difference between revisions of "Easter egg"
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− | + | * '''Description:''' enolase, glycolytic/ gluconeogenic enzyme, [[universally conserved protein]]<br/><br/> | |
+ | |||
+ | {| align="right" border="1" cellpadding="2" | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
+ | |''eno'' | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"| '''Product''' || enolase | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis/ gluconeogenesis | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46,4 kDa, 4.49 | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1290 bp, 430 amino acids | ||
+ | |- | ||
+ | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvbK]]'', ''[[pgm]]'' | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB15395]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | ||
+ | |- | ||
+ | |colspan="2" | '''Genetic context''' <br/> [[Image:eno_context.gif]] | ||
+ | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |} | ||
+ | |||
+ | __TOC__ | ||
+ | |||
+ | <br/><br/><br/><br/><br/><br/> | ||
+ | |||
+ | |||
+ | =The gene= | ||
+ | |||
+ | === Basic information === | ||
+ | |||
+ | * '''Locus tag:''' BSU33900 | ||
+ | |||
+ | ===Phenotypes of a mutant === | ||
+ | * no growth on LB, requires glucose and malate | ||
+ | * essential according to Kobayashi et al. on LB [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] | ||
+ | |||
+ | === Database entries === | ||
+ | |||
+ | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html] | ||
+ | |||
+ | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10899] | ||
+ | |||
+ | === Additional information=== | ||
+ | |||
+ | =The protein= | ||
+ | |||
+ | === Basic information/ Evolution === | ||
+ | |||
+ | * '''Catalyzed reaction/ biological activity:''' 2-phospho-D-glycerate = phosphoenolpyruvate + H<sub>2</sub>O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O | ||
+ | |||
+ | * '''Protein family:''' enolase family (according to Swiss-Prot) | ||
+ | |||
+ | * '''Paralogous protein(s):''' | ||
+ | |||
+ | === Extended information on the protein === | ||
+ | |||
+ | * '''Kinetic information:''' reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed] | ||
+ | |||
+ | * '''Domains:''' | ||
+ | ** substrate binding domain (366–369) | ||
+ | |||
+ | * '''Modification:''' phosphorylation on Thr-141 AND Ser-259 AND Tyr-281 AND Ser-325 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
+ | |||
+ | * '''Cofactor(s):''' Mg2+ | ||
+ | |||
+ | * '''Effectors of protein activity:''' | ||
+ | ** Inhibited by EDTA [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed] | ||
+ | |||
+ | * '''Interactions:''' [[Eno]]-[[PfkA]] {{PubMed|19193632}}, [[Eno]]-[[Rny]] {{PubMed|19193632}}, [[Eno]]-[[CshA]] {{PubMed|20572937}} | ||
+ | |||
+ | * '''Localization:''' cytoplasm [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] and membrane associated [http://www.ncbi.nlm.nih.gov/sites/entrez/18763711 PubMed], exported {{PubMed|15003462}} | ||
+ | |||
+ | === Database entries === | ||
+ | |||
+ | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1W6T 1W6T] (from ''Streptococcus pneumoniae'') {{PubMed|15476816}} | ||
+ | |||
+ | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37869 P37869] | ||
+ | |||
+ | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU33900] | ||
+ | |||
+ | * '''E.C. number:''' [http://www.expasy.org/enzyme/4.2.1.11 4.2.1.11] | ||
+ | |||
+ | === Additional information=== | ||
+ | * Enolase is a [[moonlighting proteins|moonlighting protein]]. [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed] | ||
+ | * There are indications that this enzyme is an octamer [http://www.ncbi.nlm.nih.gov/sites/entrez/25885 PubMed] | ||
+ | * [[universally conserved protein]] | ||
+ | |||
+ | =Expression and regulation= | ||
+ | |||
+ | * '''Operon:''' | ||
+ | ** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}} | ||
+ | ** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}} | ||
+ | |||
+ | * '''Sigma factor:''' [[SigA]] {{PubMed|11489127}} | ||
+ | |||
+ | * '''Regulation:''' | ||
+ | ** expression activated by glucose (3.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
+ | ** ''[[cggR]]'': induced by glycolytic substrates [[CggR]] {{PubMed|11489127}} | ||
+ | ** ''[[pgk]]'': constitutive {{PubMed|11489127}} | ||
+ | |||
+ | * '''Regulatory mechanism:''' transcription repression by [[CggR]] {{PubMed|11489127}} | ||
+ | |||
+ | * '''Additional information:''' | ||
+ | |||
+ | =Biological materials = | ||
+ | |||
+ | * '''Mutant:''' | ||
+ | ** GP594 (''eno''::''cat''), available in [[Stülke]] lab | ||
+ | ** GP599 (''eno''::''erm''), available in [[Stülke]] lab | ||
+ | ** GP698 (''eno''-''[[pgm]]''::''cat''), available in [[Stülke]] lab | ||
+ | |||
+ | * '''Expression vector:''' | ||
+ | ** pGP1426 (expression of ''eno'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab | ||
+ | ** pGP399 (expression of ''eno'' from ''E. coli'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab | ||
+ | ** pGP563 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab | ||
+ | ** pGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [[SPINE]], in [[pGP380]]), available in [[Stülke]] lab | ||
+ | ** pGP1500 (expression of ''[[pgm]]'' and ''[[eno]]'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab | ||
+ | |||
+ | * '''lacZ fusion:''' | ||
+ | ** see ''[[pgk]]'' | ||
+ | |||
+ | * '''GFP fusion:''' pHT315-yfp-eno, available in [[Mijakovic]] lab | ||
+ | |||
+ | * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab | ||
+ | |||
+ | * '''Antibody:''' available in [[Stülke]] lab | ||
+ | |||
+ | =Labs working on this gene/protein= | ||
+ | |||
+ | [[Stülke|Jörg Stülke]], University of Göttingen, Germany | ||
+ | [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage] | ||
+ | |||
+ | =Your additional remarks= | ||
+ | |||
+ | =References= | ||
+ | ==Reviews== | ||
+ | <pubmed> 8994873 </pubmed> | ||
+ | ==Subcellular localization of enolase== | ||
+ | <pubmed> 16479537 18763711 15003462 20497499 </pubmed> | ||
+ | ==Other original publications== | ||
+ | <pubmed> 17726680, 17218307, 12850135, 19193632, 11489127, 8021172, 17505547, 25885, 20572937 15476816 9988532 </pubmed> | ||
+ | |||
+ | [[Category:Protein-coding genes]] |
Revision as of 13:12, 29 November 2010
- Description: enolase, glycolytic/ gluconeogenic enzyme, universally conserved protein
Gene name | eno |
Synonyms | |
Essential | no |
Product | enolase |
Function | enzyme in glycolysis/ gluconeogenesis |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 46,4 kDa, 4.49 |
Gene length, protein length | 1290 bp, 430 amino acids |
Immediate neighbours | yvbK, pgm |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU33900
Phenotypes of a mutant
- no growth on LB, requires glucose and malate
- essential according to Kobayashi et al. on LB PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
- Protein family: enolase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: reversible Michaelis-Menten PubMed
- Domains:
- substrate binding domain (366–369)
- Cofactor(s): Mg2+
- Effectors of protein activity:
- Inhibited by EDTA PubMed
Database entries
- UniProt: P37869
- KEGG entry: [3]
- E.C. number: 4.2.1.11
Additional information
- Enolase is a moonlighting protein. PubMed
- There are indications that this enzyme is an octamer PubMed
- universally conserved protein
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- pGP1426 (expression of eno in B. subtilis, in pBQ200), available in Stülke lab
- pGP399 (expression of eno from E. coli in B. subtilis, in pBQ200), available in Stülke lab
- pGP563 (N-terminal His-tag, in pWH844), available in Stülke lab
- pGP93 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
- pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
- lacZ fusion:
- see pgk
- GFP fusion: pHT315-yfp-eno, available in Mijakovic lab
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Stülke lab
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Subcellular localization of enolase
Carsten Jers, Malene Mejer Pedersen, Dafni Katerina Paspaliari, Wolfgang Schütz, Christina Johnsson, Boumediene Soufi, Boris Macek, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.
Mol Microbiol: 2010, 77(2);287-99
[PubMed:20497499]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P p)
Grégory Boël, Vianney Pichereau, Ivan Mijakovic, Alain Mazé, Sandrine Poncet, Sylvie Gillet, Jean-Christophe Giard, Axel Hartke, Yanick Auffray, Josef Deutscher
Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?
J Mol Biol: 2004, 337(2);485-96
[PubMed:15003462]
[WorldCat.org]
[DOI]
(P p)
Other original publications