Difference between revisions of "FbaA"

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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
+
* '''Catalyzed reaction/ biological activity:''' D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate (according to Swiss-Prot) D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
  
 
* '''Protein family:''' class II fructose-bisphosphate aldolase family (according to Swiss-Prot) class II fructose-bisphosphate aldolase family
 
* '''Protein family:''' class II fructose-bisphosphate aldolase family (according to Swiss-Prot) class II fructose-bisphosphate aldolase family

Revision as of 15:58, 24 May 2009

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

Gene name fbaA
Synonyms fba, fba1, tsr
Essential yes
Product fructose-1,6-bisphosphate aldolase
Function enzyme in glycolysis/ gluconeogenesis
MW, pI 30,2 kDa, 5.03
Gene length, protein length 855 bp, 285 amino acids
Immediate neighbours spo0F, ywjH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FbaA context.gif
This image was kindly provided by SubtiList




The gene

Basic information

  • Coordinates: 3807538 - 3808392

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate (according to Swiss-Prot) D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
  • Protein family: class II fructose-bisphosphate aldolase family (according to Swiss-Prot) class II fructose-bisphosphate aldolase family
  • Paralogous protein(s): FbaB

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 2 x Dihydroxyacetone phosphate binding domain (210–212), (231–234)
  • Modification: phosphorylation on Thr-212 AND Thr-234 PubMed
  • Cofactor(s): 2 x zinc ion
  • Effectors of protein activity: inhibited by alpha-keto acids PubMed
  • Interactions:
  • Localization:

Database entries

  • Structure:

Additional information

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution

Expression and regulation

  • Sigma factor:
  • Regulation: constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector: pGP395 (N-terminal His-tag, in pWH844), pGP88 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380)
  • lacZ fusion: pGP601 (in pAC6)
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

  1. Trach K, Chapman JW & Piggot P (1988) Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome J Bacteriol. 170: 4194-4208. PubMed
  2. Ludwig H, Homuth G & Schmalisch M (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon Mol Microbiol. 41: 409-422. PubMed
  3. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed