Ambox notice.png

GONUTS is under stress! The website is currently experiencing long-wait times and frequent time-outs due to the record number of students, groups, and annotations related to CACAO this semester. We are currently working on increasing performance -- please accept our apologies for the technical difficulties.

You can help reduce stress on the server by:

  1. not reloading pages frequently - this just adds
  2. opening links in new windows (so you can read the old page)

ECOLI:ALF

From GONUTS
Jump to: navigation, search

Contents

Species (Taxon ID) Escherichia coli (strain K12). (taxon: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 Identifier ALF_ECOLI
UniProt Accessions P0AB71, P11604, Q2M9R7,
EMBL X14436, U28377, U00096, AP009048,
PIR S02177,
RefSeq AP_003483.1, NP_417400.1,
PDB 1B57, 1DOS, 1GYN, 1ZEN,
IntAct P0AB71,
Pfam PF01116,

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004332

fructose-bisphosphate aldolase activity

IMP: Inferred from Mutant Phenotype

F

Source: EcoliWiki

GO:0005515

protein binding

IPI: Inferred from Physical Interaction

F

Source: IntAct

GO:0008270

zinc ion binding

IDA: Inferred from Direct Assay

F

Source: EcoliWiki

GO:0006096

glycolysis

IEA: Inferred from Electronic Annotation

P

Source: UniProtKB-KW

GO:0004332

fructose-bisphosphate aldolase activity

PMID:11976750[1]

IMP: Inferred from Mutant Phenotype

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]

IMP: Inferred from Mutant Phenotype

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]

IMP: Inferred from Mutant Phenotype

F

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

complete

GO:0003824

catalytic activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

F

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006411

F

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.1.2.13

F

GO:0004332

fructose-bisphosphate aldolase activity

PMID:16562136[3]

IMP: Inferred from Mutant Phenotype

F

GO:0005515

protein binding

PMID:15690043[4]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6Y8

F

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000771

P

GO:0006096

glycolysis

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006411

P

GO:0006096

glycolysis

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0324

P

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

P

GO:0008270

zinc ion binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000771

F

GO:0008270

zinc ion binding

PMID:11985624[5]

IDA: Inferred from Direct Assay

F

GO:0008270

zinc ion binding

PMID:8436219[6]

IDA: Inferred from Direct Assay

F

GO:0016829

lyase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0456

F

GO:0016832

aldehyde-lyase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000771

F

GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F


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. 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
  4. Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed GONUTS page
  5. Katayama A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem 269: 2403-13 PubMed GONUTS page
  6. 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
Personal tools
Namespaces
Variants
Actions
Navigation
Cacao
Journal Clubs
page contributors
Toolbox