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Protein

Fructose-6-phosphate aldolase 1

Gene

fsaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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)1 Publication
  2. KM=35 mM for dihydroxyacetone (at 30 degrees Celsius and pH 8.5)1 Publication
  3. KM=0.8 mM for glyceraldehyde 3-phosphate (at 30 degrees Celsius and pH 8.5)1 Publication
  4. KM=40 mM for dihydroxyacetone (at 25 degrees Celsius and pH 8.5)1 Publication
  5. KM=11 mM for hydroxyacetone (at 25 degrees Celsius and pH 8.5)1 Publication
  6. KM=32 mM for 1-hydroxy-butan-2-one (at 25 degrees Celsius and pH 8.5)1 Publication
  7. KM=32 mM for dihydroxyacetone1 Publication
  8. KM=17.4 mM for hydroxyacetone1 Publication
  9. KM=0.197 mM for glycolaldehyde (as donor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  10. KM=62.8 mM for glycolaldehyde (as acceptor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  11. KM=0.286 mM for D-threose1 Publication
  12. KM=0.561 mM for D-arabinose-5-P1 Publication
  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)1 Publication
  2. Vmax=7 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage (at 30 degrees Celsius and pH 8.5)1 Publication
  3. Vmax=1.46 µmol/min/mg enzyme for the aldol reaction with DHA and D,L-glyceraldehyde 3-phosphate as substrates1 Publication
  4. Vmax=33.7 µmol/min/mg enzyme for the aldol reaction with HA and D,L-glyceraldehyde 3-phosphate as substrates1 Publication
  5. Vmax=0.22 µmol/min/mg enzyme for the self-aldol addition of glycolaldehyde1 Publication
  6. Vmax=0.34 µmol/min/mg enzyme for D-fructose 6-phosphate cleavage1 Publication
  7. Vmax=0.160 µmol/min/mg enzyme for D-arabinose-5-P cleavage1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei85Schiff-base intermediate with substrate2 Publications1

GO - Molecular functioni

  • fructose 6-phosphate aldolase activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processCarbohydrate metabolism
LigandSchiff base

Enzyme and pathway databases

BioCyciEcoCyc:G6428-MONOMER
MetaCyc:G6428-MONOMER
SABIO-RKiP78055

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13471 fsaA

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi85K → R: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001736431 – 220Fructose-6-phosphate aldolase 1Add BLAST220

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, 3 interactors
DIPiDIP-10218N
IntActiP78055, 1 interactor
STRINGi316385.ECDH10B_0894

Structurei

Secondary structure

1220
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 17Combined sources8
Beta strandi24 – 26Combined sources3
Helixi29 – 35Combined sources7
Helixi39 – 49Combined sources11
Turni50 – 52Combined sources3
Beta strandi54 – 59Combined sources6
Helixi65 – 78Combined sources14
Beta strandi83 – 87Combined sources5
Helixi90 – 101Combined sources12
Beta strandi106 – 111Combined sources6
Helixi114 – 123Combined sources10
Beta strandi126 – 131Combined sources6
Helixi132 – 137Combined sources6
Helixi142 – 156Combined sources15
Beta strandi161 – 165Combined sources5
Helixi170 – 178Combined sources9
Beta strandi182 – 186Combined sources5
Helixi188 – 193Combined sources6
Helixi198 – 215Combined sources18
Beta strandi216 – 218Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
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
OMAiVRHPMHV
PhylomeDBiP78055

Family and domain databases

CDDicd00956 Transaldolase_FSA, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00496 F6P_aldolase, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR023001 F6P_aldolase
IPR001585 TAL/FSA
IPR004731 Transaldolase_3B/F6P_aldolase
IPR018225 Transaldolase_AS
IPR033919 TSA/FSA_arc/bac
PANTHERiPTHR10683 PTHR10683, 1 hit
PfamiView protein in Pfam
PF00923 TAL_FSA, 1 hit
TIGRFAMsiTIGR00875 fsa_talC_mipB, 1 hit
PROSITEiView protein in PROSITE
PS01054 TRANSALDOLASE_1, 1 hit
PS00958 TRANSALDOLASE_2, 1 hit

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
PATRICifig|1411691.4.peg.1453

Similar proteinsi

Entry informationi

Entry nameiFSAA_ECOLI
AccessioniPrimary (citable) accession number: P78055
Secondary accession number(s): P77855, Q9R3X3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: March 28, 2018
This is version 149 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health