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, most abundant proteins

The gene

Basic information

• Locus tag: BSU37120

Phenotypes of a mutant

• essential PubMed, non-essential according to PubMed

Database entries

• BsubCyc: BSU37120

• 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
  • specific activity: 0.049 µmol min^-1 (mg protein)^-1 PubMed

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

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

• Cofactors: Zn2+ (Metalloenzyme)

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

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU37120

• 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
  • belongs to the 100 most abundant proteins 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

Michael Kohlstedt, Praveen K Sappa, Hanna Meyer, Sandra Maaß, Adrienne Zaprasis, Tamara Hoffmann, Judith Becker, Leif Steil, Michael Hecker, Jan Maarten van Dijl, Michael Lalk, Ulrike Mäder, Jörg Stülke, Erhard Bremer, Uwe Völker, Christoph Wittmann
Adaptation of Bacillus subtilis carbon core metabolism to simultaneous nutrient limitation and osmotic challenge: a multi-omics perspective.
Environ Microbiol: 2014, 16(6);1898-917
[PubMed:24571712] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)