FbaA

• Description: fructose 1,6-bisphosphate aldolase, glycolytic/ gluconeogenic enzyme
  
  

Gene name	fbaA
Synonyms	fba, fba1, tsr
Essential	no
Product	fructose-1,6-bisphosphate aldolase
Function	enzyme in glycolysis/ gluconeogenesis
Gene expression levels in SubtiExpress: fbaA
Metabolic function and regulation of this protein in SubtiPathways: fbaA
MW, pI	30,2 kDa, 5.03
Gene length, protein length	855 bp, 285 amino acids
Immediate neighbours	ywjH, spo0F
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, phosphoproteins

The gene

Basic information

• Locus tag: BSU37120

Phenotypes of a mutant

• essential PubMed, non-essential according to PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate (according to Swiss-Prot)

• Protein family: class II fructose-bisphosphate aldolase family (according to Swiss-Prot)
• Paralogous protein(s): FbaB

Extended information on the protein

• Kinetic information: Reversible Michaelis-Menten PubMed

• Domains:
  • 2 x Dihydroxyacetone phosphate binding domain (210–212), (231–234)

• Modification: phosphorylation on Thr-212 and Thr-234 PubMed

• Cofactor(s): Zn2+ (Metalloenzyme)

• Effectors of protein activity:
  • Inhibited by alpha-ketoglutarate, oxaloacetate and pyruvate PubMed PubMed
  • Activated by NH4+ PubMed

• Interactions:

• Localization:

Database entries

• Structure: 3Q94 (from Bacillus anthracis)

• UniProt: P13243

• KEGG entry: [3]

• E.C. number: 4.1.2.13

Additional information

• Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution
• extensive information on the structure and enzymatic properties of FbaA can be found at Proteopedia

Expression and regulation

• Operon:
  • fbaA PubMed
  • fbaA-ywjH PubMed

• Expression browser: fbaA PubMed

• Sigma factor:

• Regulation:
  • constitutively expressed PubMed
  • strongly repressed in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

• Mutant:
• GP591 (fbaA::cat), available in Jörg Stülke's lab, PubMed
• GP596 (fbaA::erm), available in Jörg Stülke's lab, PubMed

• Expression vector:
  • for expression in B. subtilis, in pBQ200: pGP1423, available in Jörg Stülke's lab
  • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP88, available in Jörg Stülke's lab
  • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP395, available in Jörg Stülke's lab

• lacZ fusion: pGP601 (in pAC6)

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• Antibody:

References

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

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)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Jun Hyuck Lee, Jungdon Bae, Dooil Kim, Yongseok Choi, Young Jun Im, Sukhoon Koh, Joong Su Kim, Mun-Kyoung Kim, Gil Bu Kang, Suk-In Hong, Dae-Sil Lee, Soo Hyun Eom
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.
Biochem Biophys Res Commun: 2006, 347(3);616-25
[PubMed:16843441] [WorldCat.org] [DOI] (P p)

Matthieu Fonvielle, Philippe Weber, Kasia Dabkowska, Michel Therisod
New highly selective inhibitors of class II fructose-1,6-bisphosphate aldolases.
Bioorg Med Chem Lett: 2004, 14(11);2923-6
[PubMed:15125960] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

S Ujita
Fructose 1,6-bisphosphate aldolases from spores and vegetative cells of Bacillus subtilis PCI 219.
J Biochem: 1978, 83(2);493-502
[PubMed:24624] [WorldCat.org] [DOI] (P p)