Difference between revisions of "CarA"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11230&redirect=T BSU11230]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/argCJBD-carAB-argF.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/argCJBD-carAB-argF.html]
Line 96: Line 97:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11230&redirect=T BSU11230]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1JDB 1JDB] (from ''Escherichia coli'', 47% identity, 64% similarity) {{PubMed|10089390}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1JDB 1JDB] (from ''Escherichia coli'', 47% identity, 64% similarity) {{PubMed|10089390}}

Revision as of 13:24, 2 April 2014

  • Description: carbamoyl-phosphate transferase-arginine (subunit A)

Gene name carA
Synonyms cpa
Essential no
Product carbamoyl-phosphate transferase-arginine (subunit A)
Function biosynthesis of arginine
Gene expression levels in SubtiExpress: carA
Interactions involving this protein in SubtInteract: CarA
Metabolic function and regulation of this protein in SubtiPathways:
carA
MW, pI 38 kDa, 6.212
Gene length, protein length 1059 bp, 353 aa
Immediate neighbours argD, carB
Sequences Protein DNA DNA_with_flanks
Genetic context
CarA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CarA expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

AhrC regulon

The gene

Basic information

  • Locus tag: BSU11230

Phenotypes of a mutant

Database entries

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

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (according to Swiss-Prot)
  • Protein family: glutamine amidotransferase type-1 domain (according to Swiss-Prot)
  • Paralogous protein(s): PyrAA

Extended information on the protein

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

Database entries

  • Structure: 1JDB (from Escherichia coli, 47% identity, 64% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

A Mountain, N H Mann, R N Munton, S Baumberg
Cloning of a Bacillus subtilis restriction fragment complementing auxotrophic mutants of eight Escherichia coli genes of arginine biosynthesis.
Mol Gen Genet: 1984, 197(1);82-9
[PubMed:6096675] [WorldCat.org] [DOI] (P p)