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Escherichia coli K-12 substr. MG1655 Enzyme: fructose bisphosphate aldolase class I



Gene: fbaB Accession Numbers: G7129 (EcoCyc), b2097, ECK2090

Synonyms: dhnA

Regulation Summary Diagram: ?

Subunit composition of fructose bisphosphate aldolase class I = [FbaB]10
         fructose bisphosphate aldolase monomer = FbaB

Summary:
The typical class I aldolases of plants and animals have been throroughly studied [Baldwin78a] Fructose-1,6-bisphosphate aldolases can be divided into two classes on the basis of their catalytic and structural properties. [Baldwin78a] Class I fructose 1,6 bisphosphate aldolases were once thought to be confined to eukaryotic organisms but have since been detected in several bacterial species. [Baldwin78] The occurence of such an aldolase in bacteria was unexpected in light of the phylogenetic distribution of aldolases. [Stribling73] The enzymes of eukaryotes generally fall into Class I and are tetramers of identical polypeptide chains. [Alefounder89a] In earlier studies [Stribling73] it was thought that the class I E. coli aldolase was typical in that it was tetrameric with a mol. wt. of approx. 140K. In 1978 new purification techniques were used.The true aldolase 1 activity could be measured by using Fru-1,6-P2 that had been purified by chromatography on DEAE-cellulose to remove the fructose-6-phosphate. Using these methods the enzyme appeared to be larger than was previously supposed and may be a decamer with a mol. wt. of approx. 340,000. The size of aldolase 1 and the effect of cross-linking reagents on it, indicate that its structure must differ significantly from that of the typical tetrameric class-I enzymes from eukaryotes. [Baldwin78, Stribling73]

Locations: cytosol, membrane

Map Position: [2,175,534 <- 2,176,586] (46.89 centisomes)
Length: 1053 bp / 350 aa

Molecular Weight of Polypeptide: 38.109 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006941 , DIP:DIP-36197N , EchoBASE:EB3815 , EcoGene:EG14062 , EcoliWiki:b2097 , ModBase:P0A991 , OU-Microarray:b2097 , PortEco:fbaB , PR:PRO_000022575 , Pride:P0A991 , Protein Model Portal:P0A991 , RefSeq:NP_416600 , RegulonDB:G7129 , SMR:P0A991 , String:511145.b2097 , UniProt:P0A991

Relationship Links: InterPro:IN-FAMILY:IPR002915 , InterPro:IN-FAMILY:IPR013785 , Pfam:IN-FAMILY:PF01791

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006096 - glycolytic process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0042802 - identical protein binding Inferred from experiment [Lasserre06]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0004332 - fructose-bisphosphate aldolase activity Inferred by computational analysis [GOA01a]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: metabolism energy metabolism, carbon glycolysis

Essentiality data for fbaB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Enzymatic reaction of: fructose bisphosphate aldolase

EC Number: 4.1.2.13

fructose 1,6-bisphosphate <=> dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: superpathway of hexitol degradation (bacteria) , superpathway of glycolysis and Entner-Doudoroff , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , gluconeogenesis I , glycolysis II (from fructose-6P) , glycolysis I (from glucose-6P)

Summary:
When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present. However the Class I enzyme is present only under these conditions. Therefore it is likely that the Class I enzyme is involved in gluconeogenesis and the class II enzyme in glycolysis. [Scamuffa80] The class I enzymes function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion. [Alefounder89a] They form a Schiff base betwen the E-amino group of a specific lysine residue in the active site and the carbonyl group of the substrate. This imine may be reduced by borohydride which therefore irreversibly inhibits class 1 aldolases in the presence of substrate. [Stribling73] The enzyme's activity was unaffected by EDTA, but it was inhibited by borohydride reduction in the presence of Fru-1,6-P2 or dihydroxyacetone phosphate. Like mammalian aldolases, it cleaved fructose 1-phosphate, albeit slowly and had a low Km for Fru-1,6-P2. Its fructose 1,6 bisphosphate cleavage activity was greatly enhanced by citrate, PEP, 2-oxoglutarate and sn-glycerol 3-phosphate. Aldolase I is very efficient at Fru-1,6-P2 cleavage when fully activated. Only a limited range of metabolites has been tested as possible activators. In contrast, its fructose 1-phosphate cleavage activity was unaffected by these compounds. The enhancement exhibited a strong dependence on pH. These novel kinetic properties do not seem to be shared by any other fructose 1,6 bisphosphate aldolase. In view of its unusual properties, it is unlikely that aldolase I from E.coli is closely related to the class-1 aldolases that have been detected in several other prokaryotes, or to the typical class I enzymes from eukaryote. [Baldwin78]

Citations: [Thomson98]

Activators (Unknown Mechanism): citrate , phosphoenolpyruvate , sn-glycerol 3-phosphate

Inhibitors (Unknown Mechanism): dihydroxyacetone phosphate , borohydride

pH(opt): 9 [BRENDA14, Baldwin78a]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Thomson98, UniProt11]
UniProt: Removed.
Chain 2 -> 350
[UniProt09]
UniProt: Fructose-bisphosphate aldolase class 1;
Sequence-Conflict 192
[Close96, UniProt10a]
Alternate sequence: L → V; UniProt: (in Ref. 1; AAB18249);
Acetylation-Modification 208
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 237
[UniProt10a]
Alternate sequence: K → A; UniProt: Loss of activity;
Active-Site 237
[UniProt10a]
UniProt: Schiff-base intermediate with dihydroxyacetone-P;
Mutagenesis-Variant 239
[UniProt10a]
Alternate sequence: K → A; UniProt: No change in activity;
Acetylation-Modification 262
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.
Sequence-Conflict 309
[Close96, UniProt10a]
Alternate sequence: N → I; UniProt: (in Ref. 1; AAB18249);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Alefounder89a: Alefounder PR, Baldwin SA, Perham RN, Short NJ (1989). "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Biochem J 1989;257(2);529-34. PMID: 2649077

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Baldwin78: Baldwin SA, Perham RN (1978). "Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);643-52. PMID: 348198

Baldwin78a: Baldwin SA, Perham RN, Stribling D (1978). "Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);633-41. PMID: 417719

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Close96: Close T.J., Choi D.W. (1996). Data submission to EMBL/GenBank/DDBJ databases on 1996-10.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Scamuffa80: Scamuffa MD, Caprioli RM (1980). "Comparison of the mechanisms of two distinct aldolases from Escherichia coli grown on gluconeogenic substrates." Biochim Biophys Acta 1980;614(2);583-90. PMID: 6996735

Stribling73: Stribling D, Perham RN (1973). "Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain)." Biochem J 1973;131(4);833-41. PMID: 4198624

Thomson98: Thomson GJ, Howlett GJ, Ashcroft AE, Berry A (1998). "The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase." Biochem J 1998;331 ( Pt 2);437-45. PMID: 9531482

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Other References Related to Gene Regulation

Lacour04: Lacour S, Landini P (2004). "SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences." J Bacteriol 186(21);7186-95. PMID: 15489429

Shimada11a: Shimada T, Yamamoto K, Ishihama A (2011). "Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli." J Bacteriol 193(3);649-59. PMID: 21115656


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc12.