Difference between revisions of "HisC"

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|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
−
|''aroJ ''
+
|''hisC ''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''hisC''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' aroJ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of aromatic amino acids
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of aromatic amino acids
 
|-
 
|-
−
|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/histidine.html His]'''
+
|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=BSU22620 hisC]
 +
|-
 +
|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=hisC hisC]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 39 kDa, 5.005   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 39 kDa, 5.005   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tyrA]]'', ''[[trpA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tyrA]]'', ''[[trpA]]''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14178&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
+
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU22620 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU22620 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU22620 DNA_with_flanks]
 
|-
 
|-
 
|-
 
|-
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:hisC_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:hisC_context.gif]]
 +
|-
 +
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hisC_2370415_2371497_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:hisC_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU22620]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/>
 +
 +
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}
  
−
<br/><br/><br/><br/>
+
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[TRAP regulon]]}}
  
 
=The gene=
 
=The gene=
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU22620&redirect=T BSU22620]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/trpEDCFBA-hisC-tyrA-aroE.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/trpEDCFBA-hisC-tyrA-aroE.html]
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=== Additional information===
 
=== Additional information===
−
 
  
 
=The protein=
 
=The protein=
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
−
* '''Interactions:'''
+
* '''[[SubtInteract|Interactions]]:'''
  
−
* '''Localization:'''
+
* '''[[Localization]]:'''
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU22620&redirect=T BSU22620]
  
−
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1UU0 1UU0] (the enzyme from ''E. coli'') {{PubMed|11518529}}
  
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P17731 P17731]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P17731 P17731]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU22620]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU22620]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.6.1.9 2.6.1.9]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.6.1.9 2.6.1.9]
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=Expression and regulation=
 
=Expression and regulation=
 +
* '''Operon:'''
 +
** ''[[aroF]]-[[aroB]]-[[aroH]]-[[trpE]]-[[trpD]]-[[trpC]]-[[trpF]]-[[trpB]]-[[trpA]]-[[hisC]]-[[tyrA]]-[[aroE]]'' (according to [http://dbtbs.hgc.jp/COG/prom/trpEDCFBA-hisC-tyrA-aroE.html DBTBS])
 +
** ''[[trpE]]-[[trpD]]-[[trpC]]-[[trpF]]-[[trpB]]-[[trpA]]-[[hisC]]-[[tyrA]]-[[aroE]]'' {{PubMed|3924737}}
 +
** ''[[hisC]]-[[tyrA]]-[[aroE]]'' (according to [http://dbtbs.hgc.jp/COG/prom/trpEDCFBA-hisC-tyrA-aroE.html DBTBS])
  
−
* '''Operon:'''  
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hisC_2370415_2371497_-1 hisC] {{PubMed|22383849}}
  
 
* '''[[Sigma factor]]:'''  
 
* '''[[Sigma factor]]:'''  
 +
** ''[[trpE]]'': [[SigA]] {{PubMed|6436812}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** induction by tryptophan ([[MtrB|TRAP]]) {{PubMed|1551827}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[MtrB|TRAP]]: binding to the mRNA in the presence of tryptophan, this results in transcription termination {{PubMed|8419914}}
  
−
* '''Additional information:'''  
+
* '''Additional information:'''
 +
** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2715 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2096 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4023 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2507 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6242 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
−
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  
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=References=
 
=References=
 +
<pubmed> 4431, 824269 11518529 3924737 6436812 1551827 8419914 21815947 23540922 </pubmed>
 +
 +
[[Category:Protein-coding genes]]

Latest revision as of 14:08, 17 April 2014

  • Description: histidinol-phosphate aminotransferase / tyrosine and phenylalanine aminotransferase

Gene name hisC
Synonyms aroJ
Essential no
Product histidinol-phosphate aminotransferase /
tyrosine and phenylalanine aminotransferase
Function biosynthesis of aromatic amino acids
Gene expression levels in SubtiExpress: hisC
Metabolic function and regulation of this protein in SubtiPathways:
hisC
MW, pI 39 kDa, 5.005
Gene length, protein length 1080 bp, 360 aa
Immediate neighbours tyrA, trpA
Sequences Protein DNA DNA_with_flanks
Genetic context
HisC context.gif
Expression at a glance   PubMed
HisC expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

  • Locus tag: BSU22620

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate (according to Swiss-Prot)
  • Protein family: bacterial solute-binding protein 3 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2715 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2096 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4023 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2507 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6242 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Martin Bommer, John M Ward
A 1-step microplate method for assessing the substrate range of l-α-amino acid aminotransferase.
Enzyme Microb Technol: 2013, 52(4-5);218-25
[PubMed:23540922] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

J Sivaraman, Y Li, R Larocque, J D Schrag, M Cygler, A Matte
Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
J Mol Biol: 2001, 311(4);761-76
[PubMed:11518529] [WorldCat.org] [DOI] (P p)

J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737] [WorldCat.org] [DOI] (P p)

H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812] [WorldCat.org] [DOI] (P p)

D A Weigent, E W Nester
Regulation of histidinol phosphate aminotransferase synthesis by tryptophan in Bacillus subtilis.
J Bacteriol: 1976, 128(1);202-11
[PubMed:824269] [WorldCat.org] [DOI] (P p)

E W Nester, A L Montoya
An enzyme common to histidine and aromatic amino acid biosynthesis in Bacillus subtilis.
J Bacteriol: 1976, 126(2);699-705
[PubMed:4431] [WorldCat.org] [DOI] (P p)

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