Latest revision as of 13:22, 29 July 2014

Description: glutamine-fructose-6-phosphate transaminase

Gene name glaube ich oder nicht	glmS
Synonyms	gcaA, ybxD
Essential	yes PubMed
Product	glutamine-fructose-6-phosphate transaminase
Function	cell wall synthesis
Metabolic function and regulation of this protein in SubtiPathways: sandbox
MW, pI	65 kDa, 4.796
Gene length, protein length	1800 bp, 600 aa
Immediate neighbours	glmM, ybbU
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context File:Quintos.gif This image was kindly provided by SubtiList
Genetic context This image was kindly provided by SubtiList
Expression at a glance PubMed

Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

This gene is a member of the following regulons

glmS ribozyme

The gene

Basic information

Locus tag: BSU01780

Phenotypes of a mutant

essential PubMed

Database entries

BsubCyc: [HELLO BSU00100]
BsubCyc: "

DBTBS entry: no entry

SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

Catalyzed reaction/ biological activity: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate (according to Swiss-Prot)

Protein family:

Paralogous protein(s):

Extended information on the protein

Kinetic information:

Domains:

Modification:

Cofactor(s):

Effectors of protein activity:

Interactions:

Localization:
- cytoplasm (according to Swiss-Prot)

Database entries

BsubCyc: [HELLO BSU00100]
BsubCyc: BSU00240

Structure:
- HIV2 (from Bacillus subtilis, 100% identity) PubMed
- 2VF4 (GlmS from E. coli, 39% identity, 58% similarity) PubMed
- the ribozyme: 3G8S, 3G9C, 3G8T, 3G95, 3G96 (all for the ribozyme from Bacillus anthracis), 2HO7 (the ribozyme from Thermonanaerobacter tengcongensis)

UniProt: P39754

KEGG entry: [2]

E.C. number: 2.6.1.16

Additional information

subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

Operon: ybbP-ybbR-glmM-glmS

Expression browser: glmS PubMed

Sigma factor: SigA PubMed

Regulation:
- repressed by glucosamine, N-acetylglucosamine, N-propionylglucosamine or N-formylglucosamine PubMed
- glmS is only expressed in the absence of glucosamine 6-phosphate (glmS ribozyme)

Regulatory mechanism: glmS ribozyme: glucosamine 6-phosphate binds the leader mRNA, and a riboswitch with ribozyme activity cleaves off the glmS section from the mRNA, resulting in stopp of transcript elongation

Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
- A ncRNA is predicted between glmM and glmS PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 2000 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 4000 PubMed

Biological materials

Mutant:

Expression vector:

lacZ fusion:

GFP fusion:

two-hybrid system:

Antibody:

Labs working on this gene/protein

Wade Winkler, University of Texas, USA, Homepage

Your additional remarks

References

Reviews

Philippe Durand, Béatrice Golinelli-Pimpaneau, Stéphane Mouilleron, Bernard Badet, Marie-Ange Badet-Denisot
Highlights of glucosamine-6P synthase catalysis.
Arch Biochem Biophys: 2008, 474(2);302-17
[PubMed:18279655] [WorldCat.org] [DOI] (I p)

The glmS Ribozyme

Krista M Brooks, Ken J Hampel
Rapid steps in the glmS ribozyme catalytic pathway: cation and ligand requirements.
Biochemistry: 2011, 50(13);2424-33
[PubMed:21395279] [WorldCat.org] [DOI] (I p)

Peter Y Watson, Martha J Fedor
The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo.
Nat Struct Mol Biol: 2011, 18(3);359-63
[PubMed:21317896] [WorldCat.org] [DOI] (I p)

Jesse C Cochrane, Sarah V Lipchock, Kathryn D Smith, Scott A Strobel
Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme.
Biochemistry: 2009, 48(15);3239-46
[PubMed:19228039] [WorldCat.org] [DOI] (I p)

Jennifer A Collins, Irnov Irnov, Stephanie Baker, Wade C Winkler
Mechanism of mRNA destabilization by the glmS ribozyme.
Genes Dev: 2007, 21(24);3356-68
[PubMed:18079181] [WorldCat.org] [DOI] (P p)

Rebecca A Tinsley, Jennifer R W Furchak, Nils G Walter
Trans-acting glmS catalytic riboswitch: locked and loaded.
RNA: 2007, 13(4);468-77
[PubMed:17283212] [WorldCat.org] [DOI] (P p)

Kenneth Blount, Izabela Puskarz, Robert Penchovsky, Ronald Breaker
Development and application of a high-throughput assay for glmS riboswitch activators.
RNA Biol: 2006, 3(2);77-81
[PubMed:17114942] [WorldCat.org] [DOI] (I p)

Daniel J Klein, Adrian R Ferré-D'Amaré
Structural basis of glmS ribozyme activation by glucosamine-6-phosphate.
Science: 2006, 313(5794);1752-6
[PubMed:16990543] [WorldCat.org] [DOI] (I p)

Ken J Hampel, Melissa M Tinsley
Evidence for preorganization of the glmS ribozyme ligand binding pocket.
Biochemistry: 2006, 45(25);7861-71
[PubMed:16784238] [WorldCat.org] [DOI] (P p)

Adam Roth, Ali Nahvi, Mark Lee, Inbal Jona, Ronald R Breaker
Characteristics of the glmS ribozyme suggest only structural roles for divalent metal ions.
RNA: 2006, 12(4);607-19
[PubMed:16484375] [WorldCat.org] [DOI] (P p)

Tom J McCarthy, Melissa A Plog, Shennen A Floy, Joshua A Jansen, Juliane K Soukup, Garrett A Soukup
Ligand requirements for glmS ribozyme self-cleavage.
Chem Biol: 2005, 12(11);1221-6
[PubMed:16298301] [WorldCat.org] [DOI] (P p)

Jeffrey E Barrick, Keith A Corbino, Wade C Winkler, Ali Nahvi, Maumita Mandal, Jennifer Collins, Mark Lee, Adam Roth, Narasimhan Sudarsan, Inbal Jona, J Kenneth Wickiser, Ronald R Breaker
New RNA motifs suggest an expanded scope for riboswitches in bacterial genetic control.
Proc Natl Acad Sci U S A: 2004, 101(17);6421-6
[PubMed:15096624] [WorldCat.org] [DOI] (P p)

Wade C Winkler, Ali Nahvi, Adam Roth, Jennifer A Collins, Ronald R Breaker
Control of gene expression by a natural metabolite-responsive ribozyme.
Nature: 2004, 428(6980);281-6
[PubMed:15029187] [WorldCat.org] [DOI] (I p)

Other Original Publications

Additional publications: PubMed

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Stéphane Mouilleron, Marie-Ange Badet-Denisot, Béatrice Golinelli-Pimpaneau
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel.
J Mol Biol: 2008, 377(4);1174-85
[PubMed:18295797] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

K Yoshida, K Kobayashi, Y Miwa, C M Kang, M Matsunaga, H Yamaguchi, S Tojo, M Yamamoto, R Nishi, N Ogasawara, T Nakayama, Y Fujita
Combined transcriptome and proteome analysis as a powerful approach to study genes under glucose repression in Bacillus subtilis.
Nucleic Acids Res: 2001, 29(3);683-92
[PubMed:11160890] [WorldCat.org] [DOI] (I p)

C J BATES, C A PASTERNAK
FURTHER STUDIES ON THE REGULATION OF AMINO SUGAR METABOLISM IN BACILLUS SUBTILIS.
Biochem J: 1965, 96(1);147-54
[PubMed:14343123] [WorldCat.org] [DOI] (P p)

@@ Line 1: / Line 1: @@
-* '''Description:''' inhibition of the pro-sigma-K processing machinery <br/><br/>
+* '''Description:''' glutamine-fructose-6-phosphate transaminase <br/><br/>
 {| align="right" border="1" cellpadding="2"
 |-
-|style="background:#ABCDEF;" align="center"|'''Gene name'''
+|style="background:#ABCDEF;" align="center"|'''Gene name''' glaube ich oder nicht
-|''bofA''
+|''glmS''
 |-
-|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
+|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''gcaA, ybxD ''
 |-
-|style="background:#ABCDEF;" align="center"| '''Essential''' || no
+|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 |-
-|style="background:#ABCDEF;" align="center"| '''Product''' || inhibitor of pro-[[SigK]] processing
+|style="background:#ABCDEF;" align="center"| '''Product''' || glutamine-fructose-6-phosphate transaminase
 |-
-|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigK]] activation
+|style="background:#ABCDEF;" align="center"|'''Function''' || cell wall synthesis
 |-
-|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00230 bofA]
+|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=sandbox sandbox]'''
 |-
-|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=BofA BofA]
+|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 65 kDa, 4.796
 |-
-|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 8 kDa, 9.32
+|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1800 bp, 600 aa
 |-
-|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 261 bp, 87 aa
+|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glmM]]'', ''[[ybbU]]''
 |-
-|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yaaL]]'', ''[[rrnA-16S]]''
+|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB11954&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
-|-
-|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU00230 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU00230 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU00230 DNA_with_flanks]
 |-
+|colspan="2" | '''Genetic context''' <br/> [[Image:quintos.gif]]
+ <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 |-
 |-
-|colspan="2" | '''Genetic context''' <br/> [[Image:bofA_context.gif]]
+|colspan="2" | '''Genetic context''' <br/> [[Image:test.gif]]
   <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 |-
-|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bofA_29772_30035_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:bofA_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00230]]
+|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glmS_200277_202079_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:glmS_expression.png|500px]]
 |-
 |}
@@ Line 39: / Line 39: @@
 <br/><br/><br/><br/>
 <br/><br/><br/><br/>
+<br/><br/><br/><br/>
+<br/><br/><br/><br/>
 <br/><br/>
 = [[Categories]] containing this gene/protein =
-{{SubtiWiki category|[[sigma factors and their control]]}},
+{{SubtiWiki category|[[cell wall synthesis]]}},
-{{SubtiWiki category|[[sporulation proteins]]}},
+{{SubtiWiki category|[[biosynthesis of cell wall components]]}},
-{{SubtiWiki category|[[membrane proteins]]}}
+{{SubtiWiki category|[[essential genes]]}}
 = This gene is a member of the following [[regulons]] =
-{{SubtiWiki regulon|[[SigE regulon]]}},
+{{SubtiWiki regulon|[[glmS ribozyme]]}}
-{{SubtiWiki regulon|[[SpoIIID regulon]]}}
 =The gene=
@@ Line 54: / Line 57: @@
 === Basic information ===
-* '''Locus tag:''' BSU00230
+* '''Locus tag:''' BSU01780
 ===Phenotypes of a mutant ===
+essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 === Database entries ===
+* '''BsubCyc:''' [HELLO BSU00100]
+* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00240&redirect=T"]
-* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/bofA.html]
+* '''DBTBS entry:''' no entry
-* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10087]
+* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10948]
 === Additional information===
 =The protein=
@@ Line 71: / Line 77: @@
 === Basic information/ Evolution ===
-* '''Catalyzed reaction/ biological activity:'''
+* '''Catalyzed reaction/ biological activity:''' L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate (according to Swiss-Prot)
 * '''Protein family:'''
@@ Line 90: / Line 96: @@
 * '''[[SubtInteract|Interactions]]:'''
-** [[BofA]]-[[SpoIVB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15292188 PubMed]
-** [[SpoIVFB]]-[[BofA]], to inhibit proteolytic activity of [[SpoIVFB]] {{PubMed|15087499}}
-** [[SpoIVFA]]-[[BofA]], recruitment of [[BofA]] to [[SpoIVFB]] {{PubMed|11959848}}
 * '''[[Localization]]:'''
-** forespore outer membrane (according to Swiss-Prot)
+** cytoplasm (according to Swiss-Prot)
-** integral membrane protein {{PubMed|11959848}}
 === Database entries ===
+* '''BsubCyc:''' [HELLO BSU00100]
+* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00240&redirect=T BSU00240]
 * '''Structure:'''
+**[http://www.pdb.org/pdb/explore/explore.do?structureId=HIV2 HIV2] (from ''Bacillus subtilis'', 100% identity) {{PubMed|13454352}}
+** [http://www.pdb.org/pdb/explore/explore.do?structureId=2VF4 2VF4] (GlmS from ''E. coli'', 39% identity, 58% similarity) {{PubMed|18295797}}
+** the ribozyme: [http://www.rcsb.org/pdb/explore.do?structureId=3g8s 3G8S], [http://www.rcsb.org/pdb/explore.do?structureId=3G9C 3G9C], [http://www.rcsb.org/pdb/explore.do?structureId=3g8t 3G8T], [http://www.rcsb.org/pdb/explore.do?structureId=3g95 3G95], [http://www.rcsb.org/pdb/explore.do?structureId=3g96 3G96] (all for the ribozyme from ''Bacillus anthracis''), [http://www.rcsb.org/pdb/explore.do?structureId=2HO7 2HO7] (the ribozyme from ''Thermonanaerobacter tengcongensis'')
-* '''UniProt:''' [http://www.uniprot.org/uniprot/P24282 P24282]
+* '''UniProt:''' [http://www.uniprot.org/uniprot/P39754 P39754]
-* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU00230]
+* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU01780]
-* '''E.C. number:'''
+* '''E.C. number:''' [http://www.expasy.org/enzyme/2.6.1.16 2.6.1.16]
 === Additional information===
+:* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 =Expression and regulation=
-* '''Operon:''' ''bofA'' [http://www.ncbi.nlm.nih.gov/sites/entrez/1315731 PubMed]
+* '''Operon:''' ''[[ybbP]]-[[ybbR]]-[[glmM]]-[[glmS]]''
-* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bofA_29772_30035_1 bofA] {{PubMed|22383849}}
+* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glmS_200277_202079_1 glmS] {{PubMed|22383849}}
-* '''Sigma factor:''' [[SigE]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1315731 PubMed]
+* '''Sigma factor:''' [[SigA]] {{PubMed|22211522}}
-* '''Regulation:''' expressed during sporulation  [http://www.ncbi.nlm.nih.gov/sites/entrez/1315731 PubMed]
+* '''Regulation:'''
+** repressed by glucosamine, N-acetylglucosamine, N-propionylglucosamine or N-formylglucosamine {{PubMed|14343123}}
+** ''glmS'' is only expressed in the absence of glucosamine 6-phosphate ([[glmS]] [[ribozyme]])
-* '''Regulatory mechanism:''' repressed by [[SpoIIID]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1315731 PubMed]
+* '''Regulatory mechanism:''' ''glmS'' [[ribozyme]]: glucosamine 6-phosphate binds the leader mRNA, and a [[riboswitch]] with [[ribozyme]] activity cleaves off the ''[[glmS]]'' section from the mRNA, resulting in stopp of transcript elongation
-* '''Additional information:''' the mRNA is very stable (half-life > 15 min) [http://www.ncbi.nlm.nih.gov/sites/entrez/12884008 PubMed]
+* '''Additional information:'''
+** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
+** A [[ncRNA]] is predicted between ''[[glmM]]'' and ''[[glmS]]'' {{PubMed|20525796}}
+** number of protein molecules per cell (minimal medium with glucose and ammonium): 2000 {{PubMed|24696501}}
+** number of protein molecules per cell (complex medium with amino acids, without glucose): 4000 {{PubMed|24696501}}
 =Biological materials =
 * '''Mutant:'''
-** 1S100 ( ''bofA''::''cat''), {{PubMed|1577688}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S100&Search=1S100 BGSC]
-** 1S96 ( ''bofA''::''erm''), {{PubMed|1315731}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S96&Search=1S96 BGSC]
 * '''Expression vector:'''
@@ Line 142: / Line 154: @@
 =Labs working on this gene/protein=
-Simon Cutting, London, UK [http://personal.rhul.ac.uk/uhba/009/bacillus/simon_cutting.html homepage]
+[[Wade Winkler]], University of Texas, USA, [http://www.utsouthwestern.edu/findfac/professional/0,,68018,00.html Homepage]
 =Your additional remarks=
 =References=
+==Reviews==
+<pubmed> 18279655 </pubmed>
-<pubmed>11959848, 9501233, 1577688, 15292188, 2115401, 12940997, 12884008,, 15292188 1315731, 15752199 16818230 15087499</pubmed>
+==The ''glmS'' Ribozyme==
+<pubmed>18079181 ,16484375, 16784238 ,15096624 , 16990543 ,17114942 ,16484375 , 15029187, 17283212 , 16298301, 19228039 21317896 21395279 </pubmed>
+==Other Original Publications==
+'''Additional publications:''' {{PubMed|22211522}}
+<pubmed> 14343123 17981983 ,11160890, 18295797 20525796  </pubmed>
 [[Category:Protein-coding genes]]

Difference between revisions of "Sandbox"

Latest revision as of 13:22, 29 July 2014

Contents

Categories containing this gene/protein

This gene is a member of the following regulons

The gene

Basic information

Phenotypes of a mutant

Database entries

Additional information

The protein

Basic information/ Evolution

Extended information on the protein

Database entries

Additional information

Expression and regulation

Biological materials

Labs working on this gene/protein

Your additional remarks

References

Reviews

The glmS Ribozyme

Other Original Publications

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