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
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 15625 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 45663 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: