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Protein

Fructose-bisphosphate aldolase class 2

Gene

fbaA

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

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

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.1 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.

  1. KM=0.17 mM for fructose-1,6-bisphosphate1 Publication
  2. KM=0.35 mM for tagatose-1,6-bisphosphate1 Publication

    Pathwayi: glycolysis

    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:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase (pgi)
    3. ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA)
    4. Fructose-bisphosphate aldolase class 2 (fbaA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    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 keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei62Glyceraldehyde 3-phosphateCurated1
    Active sitei110Proton donor1 Publication1
    Metal bindingi111Zinc 1; catalytic3 Publications1
    Metal bindingi145Zinc 23 Publications1
    Metal bindingi175Zinc 23 Publications1
    Metal bindingi227Zinc 1; catalytic3 Publications1
    Binding sitei228Dihydroxyacetone phosphate; via amide nitrogen1
    Metal bindingi265Zinc 1; catalytic3 Publications1

    GO - Molecular functioni

    • fructose-bisphosphate aldolase activity Source: EcoCyc
    • zinc ion binding Source: EcoliWiki

    GO - Biological processi

    • gluconeogenesis Source: GO_Central
    • glycolytic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:FRUCTBISALD-CLASSII-MONOMER.
    ECOL316407:JW2892-MONOMER.
    MetaCyc:FRUCTBISALD-CLASSII-MONOMER.
    BRENDAi4.1.2.13. 2026.
    SABIO-RKP0AB71.
    UniPathwayiUPA00109; 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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10282. fbaA.

    Subcellular locationi

    GO - Cellular componenti

    • cell wall Source: GO_Central
    • cytosol Source: EcoCyc
    • plasma membrane Source: GO_Central
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi36N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi60Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi62S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi62S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi108H → A: Loss of activity. 1 Publication1
    Mutagenesisi111H → A: Loss of activity. 1 Publication1
    Mutagenesisi112C → A: Partial loss of activity. 1 Publication1
    Mutagenesisi326K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL4912.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved3 Publications
    ChainiPRO_00001787132 – 359Fructose-bisphosphate aldolase class 2Add BLAST358

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei9N6-acetyllysine; alternate1 Publication1
    Modified residuei9N6-malonyllysine; alternate1 Publication1
    Modified residuei9N6-succinyllysine; alternate1 Publication1
    Modified residuei72N6-succinyllysine1 Publication1
    Modified residuei115N6-succinyllysine1 Publication1
    Modified residuei231N6-succinyllysine1 Publication1
    Modified residuei251N6-succinyllysine1 Publication1
    Modified residuei319N6-succinyllysine1 Publication1
    Modified residuei326N6-succinyllysine1 Publication1
    Modified residuei348N6-succinyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP0AB71.
    PaxDbiP0AB71.
    PRIDEiP0AB71.

    2D gel databases

    SWISS-2DPAGEP0AB71.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaKP0A6Y82EBI-370916,EBI-542092

    Protein-protein interaction databases

    BioGridi4262069. 17 interactors.
    851736. 1 interactor.
    DIPiDIP-31872N.
    IntActiP0AB71. 7 interactors.
    STRINGi511145.b2925.

    Chemistry databases

    BindingDBiP0AB71.

    Structurei

    Secondary structure

    1359
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 6Combined sources3
    Beta strandi10 – 12Combined sources3
    Helixi16 – 27Combined sources12
    Beta strandi32 – 36Combined sources5
    Helixi40 – 53Combined sources14
    Beta strandi57 – 61Combined sources5
    Helixi63 – 70Combined sources8
    Helixi81 – 97Combined sources17
    Helixi98 – 100Combined sources3
    Beta strandi104 – 109Combined sources6
    Helixi114 – 116Combined sources3
    Helixi117 – 134Combined sources18
    Beta strandi140 – 144Combined sources5
    Helixi151 – 167Combined sources17
    Beta strandi171 – 175Combined sources5
    Helixi200 – 211Combined sources12
    Beta strandi217 – 220Combined sources4
    Helixi232 – 234Combined sources3
    Helixi240 – 253Combined sources14
    Beta strandi262 – 264Combined sources3
    Helixi272 – 280Combined sources9
    Beta strandi283 – 288Combined sources6
    Helixi290 – 307Combined sources18
    Helixi308 – 310Combined sources3
    Beta strandi311 – 317Combined sources7
    Beta strandi320 – 324Combined sources5
    Helixi326 – 329Combined sources4
    Helixi331 – 352Combined sources22

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1B57X-ray2.00A/B2-359[»]
    1DOSX-ray1.67A/B2-359[»]
    1GYNX-ray2.00A2-359[»]
    1ZENX-ray2.50A2-359[»]
    ProteinModelPortaliP0AB71.
    SMRiP0AB71.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB71.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni266 – 268Dihydroxyacetone phosphate binding3
    Regioni287 – 290Dihydroxyacetone phosphate binding4

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227794.
    InParanoidiP0AB71.
    KOiK01624.
    OMAiRMSKMGM.
    PhylomeDBiP0AB71.

    Family and domain databases

    CDDicd00946. FBP_aldolase_IIA. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. FBA_II.
    IPR006411. Fruct_bisP_bact.
    [Graphical view]
    PfamiPF01116. F_bP_aldolase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsiTIGR00167. cbbA. 1 hit.
    TIGR01520. FruBisAldo_II_A. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AB71-1 [UniParc]FASTAAdd to basket

    « Hide

            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
    Length:359
    Mass (Da):39,147
    Last modified:January 23, 2007 - v2
    Checksum:i7A076D9EA62FBEC4
    GO

    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.
    PIRiS02177. ADEC2A.
    RefSeqiNP_417400.1. NC_000913.3.
    WP_000034372.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75962; AAC75962; b2925.
    BAE76989; BAE76989; BAE76989.
    GeneIDi947415.
    KEGGiecj:JW2892.
    eco:b2925.
    PATRICi32121264. VBIEscCol129921_3020.

    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.
    PIRiS02177. ADEC2A.
    RefSeqiNP_417400.1. NC_000913.3.
    WP_000034372.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1B57X-ray2.00A/B2-359[»]
    1DOSX-ray1.67A/B2-359[»]
    1GYNX-ray2.00A2-359[»]
    1ZENX-ray2.50A2-359[»]
    ProteinModelPortaliP0AB71.
    SMRiP0AB71.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262069. 17 interactors.
    851736. 1 interactor.
    DIPiDIP-31872N.
    IntActiP0AB71. 7 interactors.
    STRINGi511145.b2925.

    Chemistry databases

    BindingDBiP0AB71.
    ChEMBLiCHEMBL4912.

    2D gel databases

    SWISS-2DPAGEP0AB71.

    Proteomic databases

    EPDiP0AB71.
    PaxDbiP0AB71.
    PRIDEiP0AB71.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75962; AAC75962; b2925.
    BAE76989; BAE76989; BAE76989.
    GeneIDi947415.
    KEGGiecj:JW2892.
    eco:b2925.
    PATRICi32121264. VBIEscCol129921_3020.

    Organism-specific databases

    EchoBASEiEB0278.
    EcoGeneiEG10282. fbaA.

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227794.
    InParanoidiP0AB71.
    KOiK01624.
    OMAiRMSKMGM.
    PhylomeDBiP0AB71.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.
    BioCyciEcoCyc:FRUCTBISALD-CLASSII-MONOMER.
    ECOL316407:JW2892-MONOMER.
    MetaCyc:FRUCTBISALD-CLASSII-MONOMER.
    BRENDAi4.1.2.13. 2026.
    SABIO-RKP0AB71.

    Miscellaneous databases

    EvolutionaryTraceiP0AB71.
    PROiP0AB71.

    Family and domain databases

    CDDicd00946. FBP_aldolase_IIA. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. FBA_II.
    IPR006411. Fruct_bisP_bact.
    [Graphical view]
    PfamiPF01116. F_bP_aldolase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsiTIGR00167. cbbA. 1 hit.
    TIGR01520. FruBisAldo_II_A. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiALF_ECOLI
    AccessioniPrimary (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: November 30, 2016
    This is version 100 of the entry and version 2 of the sequence. [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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.