Difference between revisions of "FbaA"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 20: Line 20:
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 855 bp, 285 amino acids
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 855 bp, 285 amino acids
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spo0F]]'', ''[[ywjH]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ywjH]]'', ''[[spo0F]]''
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15729&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15729&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 13:27, 7 December 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
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 30,2 kDa, 5.03
Gene length, protein length 855 bp, 285 amino acids
Immediate neighbours ywjH, spo0F
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

  • Locus tag: BSU37120

Phenotypes of a mutant

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)
  • 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:
  • KEGG entry: [3]

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

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)

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)

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)