UniProtKB - P0AB71 (ALF_ECOLI)
Protein
Fructose-bisphosphate aldolase class 2
Gene
fbaA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.1 Publication
Catalytic activityi
- β-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate1 PublicationEC:4.1.2.131 Publication
Cofactori
Zn2+Note: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.
Kineticsi
The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate.
- KM=0.17 mM for fructose-1,6-bisphosphate1 Publication
- KM=0.35 mM for tagatose-1,6-bisphosphate1 Publication
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.Proteins known to be involved in the 4 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi)
- ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA), ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB)
- Fructose-bisphosphate aldolase class 2 (fbaA), Fructose-bisphosphate aldolase (fbaA)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 62 | Glyceraldehyde 3-phosphateCurated | 1 | |
Active sitei | 110 | Proton donor1 Publication | 1 | |
Metal bindingi | 111 | Zinc 1; catalytic3 Publications | 1 | |
Metal bindingi | 145 | Zinc 23 Publications | 1 | |
Metal bindingi | 175 | Zinc 23 Publications | 1 | |
Metal bindingi | 227 | Zinc 1; catalytic3 Publications | 1 | |
Binding sitei | 228 | Dihydroxyacetone phosphate; via amide nitrogen | 1 | |
Metal bindingi | 265 | Zinc 1; catalytic3 Publications | 1 |
GO - Molecular functioni
- fructose-bisphosphate aldolase activity Source: EcoCyc
- identical protein binding Source: IntAct
- zinc ion binding Source: EcoliWiki
GO - Biological processi
- gluconeogenesis Source: GO_Central
- glycolytic process Source: EcoCyc
Keywordsi
Molecular function | Lyase |
Biological process | Glycolysis |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:FRUCTBISALD-CLASSII-MONOMER MetaCyc:FRUCTBISALD-CLASSII-MONOMER |
BRENDAi | 4.1.2.13, 2026 |
SABIO-RKi | P0AB71 |
UniPathwayi | UPA00109;UER00183 |
Names & Taxonomyi
Protein namesi | Recommended name: Fructose-bisphosphate aldolase class 2 (EC:4.1.2.13)Short name: FBP aldolase Short name: FBPA Alternative name(s): Fructose-1,6-bisphosphate aldolase Fructose-bisphosphate aldolase class II |
Gene namesi | Name:fbaA Synonyms:fba, fda Ordered Locus Names:b2925, JW2892 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 36 | N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. 1 Publication | 1 | |
Mutagenesisi | 60 | Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. 1 Publication | 1 | |
Mutagenesisi | 62 | S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. 1 Publication | 1 | |
Mutagenesisi | 62 | S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. 1 Publication | 1 | |
Mutagenesisi | 108 | H → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 111 | H → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 112 | C → A: Partial loss of activity. 1 Publication | 1 | |
Mutagenesisi | 326 | K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4912 |
DrugBanki | DB03026, Phosphoglycolohydroxamic Acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed3 Publications | |||
ChainiPRO_0000178713 | 2 – 359 | Fructose-bisphosphate aldolase class 2Add BLAST | 358 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 9 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 9 | N6-malonyllysine; alternate1 Publication | 1 | |
Modified residuei | 9 | N6-succinyllysine; alternate1 Publication | 1 | |
Modified residuei | 72 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 115 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 231 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 251 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 319 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 326 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 348 | N6-succinyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0AB71 |
PaxDbi | P0AB71 |
PRIDEi | P0AB71 |
2D gel databases
SWISS-2DPAGEi | P0AB71 |
PTM databases
iPTMneti | P0AB71 |
Interactioni
Subunit structurei
Homodimer.
4 PublicationsBinary interactionsi
Hide detailsP0AB71
With | #Exp. | IntAct |
---|---|---|
dnaK [P0A6Y8] | 3 | EBI-370916,EBI-542092 |
itself | 4 | EBI-370916,EBI-370916 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4262069, 20 interactors 851736, 2 interactors |
DIPi | DIP-31872N |
IntActi | P0AB71, 7 interactors |
STRINGi | 511145.b2925 |
Chemistry databases
BindingDBi | P0AB71 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0AB71 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AB71 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 266 – 268 | Dihydroxyacetone phosphate binding | 3 | |
Regioni | 287 – 290 | Dihydroxyacetone phosphate binding | 4 |
Sequence similaritiesi
Belongs to the class II fructose-bisphosphate aldolase family.Curated
Phylogenomic databases
eggNOGi | COG0191, Bacteria |
HOGENOMi | CLU_036923_0_0_6 |
InParanoidi | P0AB71 |
PhylomeDBi | P0AB71 |
Family and domain databases
CDDi | cd00946, FBP_aldolase_IIA, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR000771, FBA_II IPR006411, Fruct_bisP_bact |
PANTHERi | PTHR30559, PTHR30559, 1 hit |
Pfami | View protein in Pfam PF01116, F_bP_aldolase, 1 hit |
PIRSFi | PIRSF001359, F_bP_aldolase_II, 1 hit |
TIGRFAMsi | TIGR00167, cbbA, 1 hit TIGR01520, FruBisAldo_II_A, 1 hit |
PROSITEi | View protein in PROSITE PS00602, ALDOLASE_CLASS_II_1, 1 hit PS00806, ALDOLASE_CLASS_II_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0AB71-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA
60 70 80 90 100
AKVKAPVIVQ FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH
110 120 130 140 150
YGVPVILHTD HCAKKLLPWI DGLLDAGEKH FAATGKPLFS SHMIDLSEES
160 170 180 190 200
LQENIEICSK YLERMSKIGM TLEIELGCTG GEEDGVDNSH MDASALYTQP
210 220 230 240 250
EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT ILRDSQEYVS
260 270 280 290 300
KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV
310 320 330 340 350
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF
QELNAIDVL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14436 Genomic DNA Translation: CAA32605.1 U28377 Genomic DNA Translation: AAA69092.1 U00096 Genomic DNA Translation: AAC75962.1 AP009048 Genomic DNA Translation: BAE76989.1 |
PIRi | S02177, ADEC2A |
RefSeqi | NP_417400.1, NC_000913.3 WP_000034372.1, NZ_STEB01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC75962; AAC75962; b2925 BAE76989; BAE76989; BAE76989 |
GeneIDi | 58348381 947415 |
KEGGi | ecj:JW2892 eco:b2925 |
PATRICi | fig|1411691.4.peg.3807 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14436 Genomic DNA Translation: CAA32605.1 U28377 Genomic DNA Translation: AAA69092.1 U00096 Genomic DNA Translation: AAC75962.1 AP009048 Genomic DNA Translation: BAE76989.1 |
PIRi | S02177, ADEC2A |
RefSeqi | NP_417400.1, NC_000913.3 WP_000034372.1, NZ_STEB01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1B57 | X-ray | 2.00 | A/B | 2-359 | [»] | |
1DOS | X-ray | 1.67 | A/B | 2-359 | [»] | |
1GYN | X-ray | 2.00 | A | 2-359 | [»] | |
1ZEN | X-ray | 2.50 | A | 2-359 | [»] | |
5GK3 | X-ray | 1.80 | A/B | 1-359 | [»] | |
5GK4 | X-ray | 2.00 | A/B | 1-359 | [»] | |
5GK5 | X-ray | 1.90 | A/B/C/D/E/F/G/H | 1-359 | [»] | |
5GK6 | X-ray | 1.80 | A/B | 1-359 | [»] | |
5GK7 | X-ray | 1.80 | A/B | 1-359 | [»] | |
5GK8 | X-ray | 2.00 | A/B | 1-359 | [»] | |
5VJD | X-ray | 1.70 | A/B | 2-359 | [»] | |
5VJE | X-ray | 1.65 | A/B | 2-359 | [»] | |
SMRi | P0AB71 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262069, 20 interactors 851736, 2 interactors |
DIPi | DIP-31872N |
IntActi | P0AB71, 7 interactors |
STRINGi | 511145.b2925 |
Chemistry databases
BindingDBi | P0AB71 |
ChEMBLi | CHEMBL4912 |
DrugBanki | DB03026, Phosphoglycolohydroxamic Acid |
PTM databases
iPTMneti | P0AB71 |
2D gel databases
SWISS-2DPAGEi | P0AB71 |
Proteomic databases
jPOSTi | P0AB71 |
PaxDbi | P0AB71 |
PRIDEi | P0AB71 |
Genome annotation databases
EnsemblBacteriai | AAC75962; AAC75962; b2925 BAE76989; BAE76989; BAE76989 |
GeneIDi | 58348381 947415 |
KEGGi | ecj:JW2892 eco:b2925 |
PATRICi | fig|1411691.4.peg.3807 |
Organism-specific databases
EchoBASEi | EB0278 |
Phylogenomic databases
eggNOGi | COG0191, Bacteria |
HOGENOMi | CLU_036923_0_0_6 |
InParanoidi | P0AB71 |
PhylomeDBi | P0AB71 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00183 |
BioCyci | EcoCyc:FRUCTBISALD-CLASSII-MONOMER MetaCyc:FRUCTBISALD-CLASSII-MONOMER |
BRENDAi | 4.1.2.13, 2026 |
SABIO-RKi | P0AB71 |
Miscellaneous databases
EvolutionaryTracei | P0AB71 |
PROi | PR:P0AB71 |
Family and domain databases
CDDi | cd00946, FBP_aldolase_IIA, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR000771, FBA_II IPR006411, Fruct_bisP_bact |
PANTHERi | PTHR30559, PTHR30559, 1 hit |
Pfami | View protein in Pfam PF01116, F_bP_aldolase, 1 hit |
PIRSFi | PIRSF001359, F_bP_aldolase_II, 1 hit |
TIGRFAMsi | TIGR00167, cbbA, 1 hit TIGR01520, FruBisAldo_II_A, 1 hit |
PROSITEi | View protein in PROSITE PS00602, ALDOLASE_CLASS_II_1, 1 hit PS00806, ALDOLASE_CLASS_II_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ALF_ECOLI | |
Accessioni | P0AB71Primary (citable) accession number: P0AB71 Secondary accession number(s): P11604, Q2M9R7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 8, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 132 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families