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ECOLI:ALF

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fbaA (synonyms: fba, fda)
Protein Name(s) Fructose-bisphosphate aldolase class 2

FBP aldolase FBPA Fructose-1,6-bisphosphate aldolase Fructose-bisphosphate aldolase class II

External Links
UniProt P0AB71
EMBL X14436
U28377
U00096
AP009048
PIR S02177
RefSeq NP_417400.1
YP_491125.1
PDB 1B57
1DOS
1GYN
1ZEN
PDBsum 1B57
1DOS
1GYN
1ZEN
ProteinModelPortal P0AB71
SMR P0AB71
BioGrid 851736
DIP DIP-31872N
IntAct P0AB71
STRING 511145.b2925
BindingDB P0AB71
ChEMBL CHEMBL4912
SWISS-2DPAGE P0AB71
PaxDb P0AB71
PRIDE P0AB71
EnsemblBacteria AAC75962
BAE76989
GeneID 12933075
947415
KEGG ecj:Y75_p2856
eco:b2925
PATRIC 32121264
EchoBASE EB0278
EcoGene EG10282
eggNOG COG0191
HOGENOM HOG000227794
InParanoid P0AB71
KO K01624
OMA RMSKMGM
OrthoDB EOG69GZPB
PhylomeDB P0AB71
BioCyc EcoCyc:FRUCTBISALD-CLASSII-MONOMER
ECOL316407:JW2892-MONOMER
MetaCyc:FRUCTBISALD-CLASSII-MONOMER
SABIO-RK P0AB71
UniPathway UPA00109
EvolutionaryTrace P0AB71
PRO PR:P0AB71
Proteomes UP000000318
UP000000625
Genevestigator P0AB71
GO GO:0004332
GO:0008270
GO:0006096
Gene3D 3.20.20.70
InterPro IPR013785
IPR006411
IPR000771
Pfam PF01116
PIRSF PIRSF001359
TIGRFAMs TIGR00167
TIGR01520
PROSITE PS00602
PS00806

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004332

fructose-bisphosphate aldolase activity

PMID:11976750[1]

ECO:0000315

F

Table 2. Aldolase activity is greatly reduced when a mutant strain of E. coli containing a temperature sensitive form of fbaA is incubated at 42 degrees Celsius, thus rendering the gene inactive.

complete

GO:0006096

glycolysis

PMID:11976750[1]

ECO:0000315

P

Table 2. A mutant strain of E. coli containing a temperature sensitive form of fbaA is unable to grow on galactitol when incubated at 42 degrees Celsius(fbaA is inactive at this temperature).

complete

GO:0004332

fructose-bisphosphate aldolase activity

PMID:368027[2]

ECO:0000315

F

Table 4. The overexpression of fda with a plasmid containing fda conferees a significantly higher amount of fructose-biphosphate aldolase activity.

complete

enables

GO:0008270

zinc ion binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10282
PANTHER:PTN001254576

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10282
PANTHER:PTN001254576
SGD:S000001543

P

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001254576
SGD:S000001543

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000186998
PANTHER:PTN001254576

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10282
PANTHER:PTN001254576
SGD:S000001543

C

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10282
PANTHER:PTN001254576
SGD:S000001543

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:8939754[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AB71

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:8836102[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AB71

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AB71

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:8436219[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:11985624[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:16562136[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:16562136[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:8436219[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:6996735[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013785

F

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006411

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006411

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771

F

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771

F

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.2.13

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Brinkkötter, A et al. (2002) Two class II D-tagatose-bisphosphate aldolases from enteric bacteria. Arch. Microbiol. 177 410-9 PubMed GONUTS page
  2. ↑ Thomson, J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J. Bacteriol. 137 502-6 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Cooper, SJ et al. (1996) The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Structure 4 1303-15 PubMed GONUTS page
  5. ↑ Blom, NS et al. (1996) Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat. Struct. Biol. 3 856-62 PubMed GONUTS page
  6. ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  7. ↑ 7.0 7.1 Berry, A & Marshall, KE (1993) Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 318 11-6 PubMed GONUTS page
  8. ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page
  9. ↑ 9.0 9.1 Böck, A & Neidhardt, FC (1966) Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. J. Bacteriol. 92 464-9 PubMed GONUTS page
  10. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  11. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  12. ↑ Scamuffa, MD & Caprioli, RM (1980) Comparison of the mechanisms of two distinct aldolases from Escherichia coli grown on gluconeogenic substrates. Biochim. Biophys. Acta 614 583-90 PubMed GONUTS page
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