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| * '''Description:''' enolase, glycolytic/ gluconeogenic enzyme<br/><br/>
| | {{#bank: Eno}} |
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| {| align="right" border="1" cellpadding="2" | |
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''eno''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Essential''' || yes
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Product''' || enolase
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| |style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis/ gluconeogenesis
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46,4 kDa, 4.49
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1290 bp, 430 amino acids
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pgm]]'', ''[[yvgK]]''
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| |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)'''
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| |colspan="2" | '''Genetic context''' <br/> [[Image:eno_context.gif]]
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| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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| |-
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| |}
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| __TOC__
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| <br/><br/>
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| =The gene=
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| === Basic information ===
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| * '''Coordinates:''' 3475589 - 3476878
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| ===Phenotypes of a mutant ===
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| essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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| === Database entries ===
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cggR-gapA-pgk-tpiA-pgm-eno.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10899]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:''' 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
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| * '''Protein family:''' enolase family (according to Swiss-Prot) enolase family
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| * '''Paralogous protein(s):'''
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''Domains:'''
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| ** substrate binding domain (366–369)
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| * '''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]
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| * '''Cofactor(s):''' magnesium ion
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| * '''Effectors of protein activity:'''
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| * '''Interactions:''' [[Eno]]-[[PfkA]], [[Eno]]-[[Rny]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed]
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| * '''Localization:''' cytoplasm (according to Swiss-Prot), cytoplasm [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] and membrane associated [http://www.ncbi.nlm.nih.gov/sites/entrez/18763711 PubMed]
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| === Database entries ===
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| * '''Structure:'''
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| * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P37869 P37869]
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| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU33900 BSU33900]
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| * '''E.C. number:''' [http://www.expasy.org/enzyme/4.2.1.11 4.2.1.11]
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| === Additional information===
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| =Expression and regulation=
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| * '''Operon:'''
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| ** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]''
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| ** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]''
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| * '''Sigma factor:''' [[SigA]]
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| * '''Regulation:''' expression activated by glucose (3.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
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| **''[[cggR]]'': neg. regulated by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed], induced by sugar
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| **''[[pgk]]'': constitutive [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed]
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| * '''Regulatory mechanism:''' transcription repression by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed]
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| * '''Additional information:'''
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| =Biological materials =
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| * '''Mutant:'''
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| * '''Expression vector:''' pGP563 (N-terminal His-tag, in [[pWH844]]), pGP93 (N-terminal Strep-tag, purification from ''B. subtilis'', for [[SPINE]], in [[pGP380]]), available in [[Stülke]] lab
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| * '''lacZ fusion:'''
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| * '''GFP fusion:''' pHT315-yfp-eno, available in [[Mijakovic]] lab
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| * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
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| * '''Antibody:''' available in [[Stülke]] lab
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| =Labs working on this gene/protein=
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| [[Stülke|Jörg Stülke]], University of Göttingen, Germany
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| [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
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| =Your additional remarks=
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| =References=
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| # Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
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| # Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in ''Bacillus subtilis''. ''Proteomics'' '''7:''' 3509-3526. [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
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| # Lévine et al. (2006) Analysis of the dynamic ''Bacillus subtilis'' Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. ''Proteomics'' '''6:''' 2157-2173 [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
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| # Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed]
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| # Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in ''Bacillus subtilis'': evidence for the presence of multiple levels of control of the ''gapA'' operon. Mol Microbiol 41, 409-422.[http://www.ncbi.nlm.nih.gov/sites/entrez/11489127 PubMed]
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| # Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. [http://www.ncbi.nlm.nih.gov/sites/entrez/17505547 PubMed]
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| # Leyva-Vazquez, M. A., and Setlow, P. (1994) Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J Bacteriol 176: 3903-3910. [http://www.ncbi.nlm.nih.gov/sites/entrez/8021172 PubMed]
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| # Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium ''Bacillus subtilis''. Mol. Cell. Proteomics 6: 697-707 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
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