Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-6-phosphate aldolase 1

Gene

fsaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D---threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.4 Publications

Catalytic activityi

D-fructose 6-phosphate = glycerone + D-glyceraldehyde 3-phosphate.4 Publications

Enzyme regulationi

Inhibited by glycerol, inorganic phosphate and arabinose 5-phosphate.1 Publication

Kineticsi

kcat is 1.31 sec(-1), 0.82 sec(-1) and 0.63 sec(-1) using glyceraldehyde 3-phosphate as acceptor substrate, and dihydroxyacetone, hydroxyacetone or 1-hydroxy-butan-2-one as donor substrate, respectively (at 25 degrees Celsius and pH 8.5).1 Publication

  1. KM=9 mM for D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5) (PubMed:11120740 and PubMed:19554584)3 Publications
  2. KM=35 mM for dihydroxyacetone (at 30 degrees Celsius and pH 8.5)3 Publications
  3. KM=0.8 mM for glyceraldehyde 3-phosphate (at 30 degrees Celsius and pH 8.5)3 Publications
  4. KM=40 mM for dihydroxyacetone (at 25 degrees Celsius and pH 8.5)3 Publications
  5. KM=11 mM for hydroxyacetone (at 25 degrees Celsius and pH 8.5)3 Publications
  6. KM=32 mM for 1-hydroxy-butan-2-one (at 25 degrees Celsius and pH 8.5)3 Publications
  7. KM=32 mM for dihydroxyacetone3 Publications
  8. KM=17.4 mM for hydroxyacetone3 Publications
  9. KM=0.197 mM for glycolaldehyde (as donor substrate in the self-aldol addition of glycolaldehyde)3 Publications
  10. KM=62.8 mM for glycolaldehyde (as acceptor substrate in the self-aldol addition of glycolaldehyde)3 Publications
  11. KM=0.286 mM for D-threose3 Publications
  12. KM=0.561 mM for D-arabinose-5-P3 Publications
  1. Vmax=45 µmol/min/mg enzyme for the aldolization reaction leading to D-fructose 6-phosphate (at 30 degrees Celsius and pH 8.5)3 Publications
  2. Vmax=7 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage (at 30 degrees Celsius and pH 8.5)3 Publications
  3. Vmax=1.46 µmol/min/mg enzyme for the aldol reaction with DHA and D,L-glyceraldehyde 3-phosphate as substrates3 Publications
  4. Vmax=33.7 µmol/min/mg enzyme for the aldol reaction with HA and D,L-glyceraldehyde 3-phosphate as substrates3 Publications
  5. Vmax=0.22 µmol/min/mg enzyme for the self-aldol addition of glycolaldehyde3 Publications
  6. Vmax=0.34 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage3 Publications
  7. Vmax=0.160 µmol/min/mg enzyme for D-arabinose-5-P cleavage3 Publications

pH dependencei

Optimum pH is about 8.5. Active from pH 6 to 12.1 Publication

Temperature dependencei

Displays a broad temperature optimum and is active in the range from 20 to 75 degrees Celsius. Although no significant loss of activity is detected after 600 hours of incubation at 45 degrees Celsius (at pH 8.0), the respective half-lives of the enzyme are 200 hours at 55 degrees Celsius, 30 hours at 65 degrees Celsius, and 16 hours at 75 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Schiff-base intermediate with substrate2 Publications

GO - Molecular functioni

  • fructose 6-phosphate aldolase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciEcoCyc:G6428-MONOMER.
ECOL316407:JW5109-MONOMER.
MetaCyc:G6428-MONOMER.
SABIO-RKP78055.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-6-phosphate aldolase 1 (EC:4.1.2.-)
Alternative name(s):
Fructose-6-phosphate aldolase A
Short name:
FSAA
Gene namesi
Name:fsaA
Synonyms:fsa, mipB, ybiZ
Ordered Locus Names:b0825, JW5109
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13471. fsaA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Is an interesting tool in chemoenzymatic synthesis for the construction of chiral complex polyhydroxylated sugar-type structures. The use of hydroxyacetone (acetol) as a donor compound allows access to various 1-deoxysugars. Can also be used for the synthesis of a broad range of iminocyclitols, that are potent glycosidase and glycosyltransferase inhibitors, from dihydroxyacetone, hydroxyacetone or 1-hydroxy-butan-2-one as donor substrate, and a range of acceptor substrates.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851K → R: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Fructose-6-phosphate aldolase 1PRO_0000173643Add
BLAST

Proteomic databases

PaxDbiP78055.
PRIDEiP78055.

Interactioni

Subunit structurei

Homodecamer. Five subunits are arranged as a pentamer, and two ring-like pentamers pack like a donut to form the decamer.2 Publications

Protein-protein interaction databases

BioGridi4263503. 2 interactions.
DIPiDIP-10218N.
IntActiP78055. 1 interaction.
STRINGi511145.b0825.

Structurei

Secondary structure

1
220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 178Combined sources
Beta strandi24 – 263Combined sources
Helixi29 – 357Combined sources
Helixi39 – 4911Combined sources
Turni50 – 523Combined sources
Beta strandi54 – 596Combined sources
Helixi65 – 7814Combined sources
Beta strandi83 – 875Combined sources
Helixi90 – 10112Combined sources
Beta strandi106 – 1116Combined sources
Helixi114 – 12310Combined sources
Beta strandi126 – 1316Combined sources
Helixi132 – 1376Combined sources
Helixi142 – 15615Combined sources
Beta strandi161 – 1655Combined sources
Helixi170 – 1789Combined sources
Beta strandi182 – 1865Combined sources
Helixi188 – 1936Combined sources
Helixi198 – 21518Combined sources
Beta strandi216 – 2183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6WX-ray1.93A/B/C/D/E/F/G/H/I/J1-220[»]
4RXFX-ray2.40A/B/C/D/E/F/G/H/I/J2-220[»]
4RXGX-ray2.15A/B/C/D/E/F/G/H/I/J1-220[»]
4RZ4X-ray1.75A/B/C/D/E/F/G/H/I/J2-220[»]
4S1FX-ray2.24A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-220[»]
ProteinModelPortaliP78055.
SMRiP78055. Positions 1-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78055.

Family & Domainsi

Sequence similaritiesi

Belongs to the transaldolase family. Type 3A subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107T9Z. Bacteria.
COG0176. LUCA.
HOGENOMiHOG000226075.
InParanoidiP78055.
KOiK08313.
OMAiIHVQVVA.
OrthoDBiEOG6PS600.
PhylomeDBiP78055.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00496. F6P_aldolase.
InterProiIPR013785. Aldolase_TIM.
IPR023001. F6P_aldolase.
IPR001585. TAL/FSA.
IPR004731. Transaldolase_3B/F6P_aldolase.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00875. fsa_talC_mipB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78055-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLD VVLPQLHEAM
60 70 80 90 100
GGQGRLFAQV MATTAEGMVN DALKLRSIIA DIVVKVPVTA EGLAAIKMLK
110 120 130 140 150
AEGIPTLGTA VYGAAQGLLS ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH
160 170 180 190 200
QLLKMHAPQA KVLAASFKTP RQALDCLLAG CESITLPLDV AQQMISYPAV
210 220
DAAVAKFEQD WQGAFGRTSI
Length:220
Mass (Da):22,997
Last modified:July 15, 1998 - v2
Checksum:i317B9A06CD19C587
GO

Mass spectrometryi

Molecular mass is 22998 Da from positions 1 - 220. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88188 Genomic DNA. Translation: BAA13552.1.
U00096 Genomic DNA. Translation: AAC73912.2.
AP009048 Genomic DNA. Translation: BAA35513.2.
PIRiA64820.
RefSeqiNP_415346.4. NC_000913.3.
WP_001336208.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73912; AAC73912; b0825.
BAA35513; BAA35513; BAA35513.
GeneIDi945449.
KEGGiecj:JW5109.
eco:b0825.
PATRICi32116853. VBIEscCol129921_0852.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88188 Genomic DNA. Translation: BAA13552.1.
U00096 Genomic DNA. Translation: AAC73912.2.
AP009048 Genomic DNA. Translation: BAA35513.2.
PIRiA64820.
RefSeqiNP_415346.4. NC_000913.3.
WP_001336208.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6WX-ray1.93A/B/C/D/E/F/G/H/I/J1-220[»]
4RXFX-ray2.40A/B/C/D/E/F/G/H/I/J2-220[»]
4RXGX-ray2.15A/B/C/D/E/F/G/H/I/J1-220[»]
4RZ4X-ray1.75A/B/C/D/E/F/G/H/I/J2-220[»]
4S1FX-ray2.24A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-220[»]
ProteinModelPortaliP78055.
SMRiP78055. Positions 1-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263503. 2 interactions.
DIPiDIP-10218N.
IntActiP78055. 1 interaction.
STRINGi511145.b0825.

Proteomic databases

PaxDbiP78055.
PRIDEiP78055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73912; AAC73912; b0825.
BAA35513; BAA35513; BAA35513.
GeneIDi945449.
KEGGiecj:JW5109.
eco:b0825.
PATRICi32116853. VBIEscCol129921_0852.

Organism-specific databases

EchoBASEiEB3244.
EcoGeneiEG13471. fsaA.

Phylogenomic databases

eggNOGiENOG4107T9Z. Bacteria.
COG0176. LUCA.
HOGENOMiHOG000226075.
InParanoidiP78055.
KOiK08313.
OMAiIHVQVVA.
OrthoDBiEOG6PS600.
PhylomeDBiP78055.

Enzyme and pathway databases

BioCyciEcoCyc:G6428-MONOMER.
ECOL316407:JW5109-MONOMER.
MetaCyc:G6428-MONOMER.
SABIO-RKP78055.

Miscellaneous databases

EvolutionaryTraceiP78055.
PROiP78055.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00496. F6P_aldolase.
InterProiIPR013785. Aldolase_TIM.
IPR023001. F6P_aldolase.
IPR001585. TAL/FSA.
IPR004731. Transaldolase_3B/F6P_aldolase.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00875. fsa_talC_mipB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Isomura M., Ogino T., Mizuno T.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases."
    Schuermann M., Sprenger G.A.
    J. Biol. Chem. 276:11055-11061(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MASS SPECTROMETRY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF LYS-85.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  6. "Fructose-6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars."
    Schuermann M., Schuermann M., Sprenger G.A.
    J. Mol. Catal., B Enzym. 19:247-252(2002)
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "D-Fructose-6-phosphate aldolase-catalyzed one-pot synthesis of iminocyclitols."
    Sugiyama M., Hong Z., Liang P.H., Dean S.M., Whalen L.J., Greenberg W.A., Wong C.H.
    J. Am. Chem. Soc. 129:14811-14817(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, BIOTECHNOLOGY.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Asymmetric self- and cross-aldol reactions of glycolaldehyde catalyzed by D-fructose-6-phosphate aldolase."
    Garrabou X., Castillo J.A., Guerard-Helaine C., Parella T., Joglar J., Lemaire M., Clapes P.
    Angew. Chem. Int. Ed. 48:5521-5525(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, BIOTECHNOLOGY.
  9. "Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family."
    Thorell S., Schurmann M., Sprenger G.A., Schneider G.
    J. Mol. Biol. 319:161-171(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS), ACTIVE SITE, SUBUNIT.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiFSAA_ECOLI
AccessioniPrimary (citable) accession number: P78055
Secondary accession number(s): P77855, Q9R3X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 20, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is not inhibited by EDTA which points to a metal-independent mode of action.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.