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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Thermus caldophilus and UniProt Accession Q703I2

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.13 fructose-bisphosphate aldolase
IUBMB Comments
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
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Thermus caldophilus
UNIPROT: Q703I2
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The taxonomic range for the selected organisms is: Thermus caldophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldolase, aldolase a, aldolase b, aldolase c, aldoa, fructose-1,6-bisphosphate aldolase, fructose-bisphosphate aldolase, aldob, fructose bisphosphate aldolase, fructose 1,6-bisphosphate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,6-Diphosphofructose aldolase
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37 kDa major allergen
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41 kDa antigen
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aldolase
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aldolase, fructose diphosphate
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-
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ALDP
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Brain-type aldolase
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-
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CE1
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CE2
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Diphosphofructose aldolase
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-
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FBP aldolase
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Fru-P2A
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Fructoaldolase
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Fructose 1,6-bisphosphate aldolase
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Fructose 1,6-diphosphate aldolase
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Fructose 1-monophosphate aldolase
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Fructose 1-phosphate aldolase
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Fructose bisphosphate aldolase
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Fructose diphosphate aldolase
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Fructose-1,6-bisphosphate triosephosphate-lyase
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IgE-binding allergen
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ketose 1-phosphate aldolase
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Liver-type aldolase
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Muscle-type aldolase
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Phosphofructoaldolase
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SMALDO
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zymohexase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-52-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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r
D-glyceraldehyde 3-phosphate + glycerone phosphate
tagatose-1,6-bisphosphate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALF_THECA
305
0
32987
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 27% polyethylene glycol 10000, 0.1M HEPES-NaOH, at pH 7.0-7.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, J.H.; Bae, J.; Kim, D.; Choi, Y.; Im, Y.J.; Koh, S.; Kim, J.S.; Kim, M.K.; Kang, G.B.; Hong, S.I.; Lee, D.S.; Eom, S.H.
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus
Biochem. Biophys. Res. Commun.
347
616-625
2006
Thermus caldophilus (Q703I2), Thermus caldophilus, Thermus caldophilus GK24 (Q703I2), Thermus caldophilus GK24
Manually annotated by BRENDA team