PycA

• Description: pyruvate carboxylase
  
  

Gene name	pycA
Synonyms	ylaP
Essential	no
Product	pyruvate carboxylase
Function	replenishment of the oxaloacetate pool
Gene expression levels in SubtiExpress: pycA
Metabolic function and regulation of this protein in SubtiPathways: pycA
MW, pI	127 kDa, 5.407
Gene length, protein length	3444 bp, 1148 aa
Immediate neighbours	ftsW, ctaA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU14860

Database entries

• BsubCyc: BSU14860

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors: biotin

• Effectors of protein activity:

• Interactions:

• Localization:
  • membrane associated PubMed
  • cytoplasm (homogeneously distributed throughout the cell) PubMed

Database entries

• BsubCyc: BSU14860

• Structure: 3BG5 (S. aureus)

• UniProt: Q9KWU4

• KEGG entry: [3]

• E.C. number: 6.4.1.1

Additional information

PycA binds to StrepTactin, and may be co-purified when purifying Strep-tagged proteins by SPINE.

PycA is subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: pycA PubMed

• Expression browser: pycA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • subject to positive stringent control upon lysine starvation PubMed

• Regulatory mechanism:
  • stringent response: due to presence of adenines at +1 and +2 positions of the transcript PubMed

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2222 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 6831 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1602 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 907 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2037 PubMed

Biological materials

• Mutant: GP793 (cat), available in Jörg Stülke's lab

• Expression vector:
  • pGP1289 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Sarawut Jitrapakdee, Martin St Maurice, Ivan Rayment, W Wallace Cleland, John C Wallace, Paul V Attwood
Structure, mechanism and regulation of pyruvate carboxylase.
Biochem J: 2008, 413(3);369-87
[PubMed:18613815] [WorldCat.org] [DOI] (I p)

Sarawut Jitrapakdee, John C Wallace
The biotin enzyme family: conserved structural motifs and domain rearrangements.
Curr Protein Pept Sci: 2003, 4(3);217-29
[PubMed:12769720] [WorldCat.org] [DOI] (P p)

S Jitrapakdee, J C Wallace
Structure, function and regulation of pyruvate carboxylase.
Biochem J: 1999, 340 ( Pt 1)(Pt 1);1-16
[PubMed:10229653] [WorldCat.org] [DOI] (P p)

J C Wallace, S Jitrapakdee, A Chapman-Smith
Pyruvate carboxylase.
Int J Biochem Cell Biol: 1998, 30(1);1-5
[PubMed:9597748] [WorldCat.org] [DOI] (P p)

P V Attwood
The structure and the mechanism of action of pyruvate carboxylase.
Int J Biochem Cell Biol: 1995, 27(3);231-49
[PubMed:7780827] [WorldCat.org] [DOI] (P p)