PycA

• Description: pyruvate carboxylase
  
  

Gene name	pycA
Synonyms	ylaP
Essential	no
Product	pyruvate carboxylase
Function	replenishment of the oxaloacetate pool
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Biotin
MW, pI	127 kDa, 5.407
Gene length, protein length	3444 bp, 1148 aa
Immediate neighbours	ftsW, ctaA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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

• 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:

• Cofactor(s): biotin

• Effectors of protein activity:

• Interactions:

• Localization: membrane associated PubMed

Database entries

• 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

Biological materials

• Mutant:

• Expression vector:

• 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)

Original publications

Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)