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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

    Pathway:iglycolysis

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621Glyceraldehyde 3-phosphateCurated
    Active sitei110 – 1101Proton donor1 Publication
    Metal bindingi111 – 1111Zinc 1; catalytic3 Publications
    Metal bindingi145 – 1451Zinc 23 Publications
    Metal bindingi175 – 1751Zinc 23 Publications
    Metal bindingi227 – 2271Zinc 1; catalytic3 Publications
    Binding sitei228 – 2281Dihydroxyacetone phosphate; via amide nitrogen
    Metal bindingi265 – 2651Zinc 1; catalytic3 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10282. fbaA.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. 1 Publication
    Mutagenesisi60 – 601Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. 1 Publication
    Mutagenesisi62 – 621S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. 1 Publication
    Mutagenesisi62 – 621S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. 1 Publication
    Mutagenesisi108 – 1081H → A: Loss of activity. 1 Publication
    Mutagenesisi111 – 1111H → A: Loss of activity. 1 Publication
    Mutagenesisi112 – 1121C → A: Partial loss of activity. 1 Publication
    Mutagenesisi326 – 3261K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 359358Fructose-bisphosphate aldolase class 2PRO_0000178713Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysine; alternate1 Publication
    Modified residuei9 – 91N6-malonyllysine; alternate1 Publication
    Modified residuei9 – 91N6-succinyllysine; alternate1 Publication
    Modified residuei72 – 721N6-succinyllysine1 Publication
    Modified residuei115 – 1151N6-succinyllysine1 Publication
    Modified residuei231 – 2311N6-succinyllysine1 Publication
    Modified residuei251 – 2511N6-succinyllysine1 Publication
    Modified residuei319 – 3191N6-succinyllysine1 Publication
    Modified residuei326 – 3261N6-succinyllysine1 Publication
    Modified residuei348 – 3481N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    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

    BioGridi851736. 1 interaction.
    DIPiDIP-31872N.
    IntActiP0AB71. 7 interactions.
    STRINGi511145.b2925.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63Combined sources
    Beta strandi10 – 123Combined sources
    Helixi16 – 2712Combined sources
    Beta strandi32 – 365Combined sources
    Helixi40 – 5314Combined sources
    Beta strandi57 – 615Combined sources
    Helixi63 – 708Combined sources
    Helixi81 – 9717Combined sources
    Helixi98 – 1003Combined sources
    Beta strandi104 – 1096Combined sources
    Helixi114 – 1163Combined sources
    Helixi117 – 13418Combined sources
    Beta strandi140 – 1445Combined sources
    Helixi151 – 16717Combined sources
    Beta strandi171 – 1755Combined sources
    Helixi200 – 21112Combined sources
    Beta strandi217 – 2204Combined sources
    Helixi232 – 2343Combined sources
    Helixi240 – 25314Combined sources
    Beta strandi262 – 2643Combined sources
    Helixi272 – 2809Combined sources
    Beta strandi283 – 2886Combined sources
    Helixi290 – 30718Combined sources
    Helixi308 – 3103Combined sources
    Beta strandi311 – 3177Combined sources
    Beta strandi320 – 3245Combined sources
    Helixi326 – 3294Combined sources
    Helixi331 – 35222Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B57X-ray2.00A/B2-359[»]
    1DOSX-ray1.67A/B2-359[»]
    1GYNX-ray2.00A2-359[»]
    1ZENX-ray2.50A2-359[»]
    ProteinModelPortaliP0AB71.
    SMRiP0AB71. Positions 2-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB71.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni266 – 2683Dihydroxyacetone phosphate binding
    Regioni287 – 2904Dihydroxyacetone phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227794.
    InParanoidiP0AB71.
    KOiK01624.
    OMAiRMSKMGM.
    OrthoDBiEOG69GZPB.
    PhylomeDBiP0AB71.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006411. Fruct_bisP_bact.
    IPR000771. Ketose_bisP_aldolase_II.
    [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_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75962; AAC75962; b2925.
    BAE76989; BAE76989; BAE76989.
    GeneIDi947415.
    KEGGieco: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_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B57X-ray2.00A/B2-359[»]
    1DOSX-ray1.67A/B2-359[»]
    1GYNX-ray2.00A2-359[»]
    1ZENX-ray2.50A2-359[»]
    ProteinModelPortaliP0AB71.
    SMRiP0AB71. Positions 2-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi851736. 1 interaction.
    DIPiDIP-31872N.
    IntActiP0AB71. 7 interactions.
    STRINGi511145.b2925.

    Chemistry

    BindingDBiP0AB71.
    ChEMBLiCHEMBL4912.

    2D gel databases

    SWISS-2DPAGEP0AB71.

    Proteomic databases

    PaxDbiP0AB71.
    PRIDEiP0AB71.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75962; AAC75962; b2925.
    BAE76989; BAE76989; BAE76989.
    GeneIDi947415.
    KEGGieco:b2925.
    PATRICi32121264. VBIEscCol129921_3020.

    Organism-specific databases

    EchoBASEiEB0278.
    EcoGeneiEG10282. fbaA.

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227794.
    InParanoidiP0AB71.
    KOiK01624.
    OMAiRMSKMGM.
    OrthoDBiEOG69GZPB.
    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

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006411. Fruct_bisP_bact.
    IPR000771. Ketose_bisP_aldolase_II.
    [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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
      Alefounder P.R., Perham R.N.
      Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / CS520.
    2. "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli."
      Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.
      Biochem. J. 257:529-534(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27.
    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. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    6. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli."
      Berry A., Marshall K.E.
      FEBS Lett. 318:11-16(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
    8. "Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases."
      Zgiby S.M., Thomson G.J., Qamar S., Berry A.
      Eur. J. Biochem. 267:1858-1868(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, REACTION MECHANISM, MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326.
      Strain: K12 / MG1655 / ATCC 47076.
    9. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    10. Cited for: MALONYLATION AT LYS-9.
      Strain: K12.
    11. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326 AND LYS-348.
      Strain: K12.
    12. "Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase."
      Blom N.S., Tetreault S., Coulombe R., Sygusch J.
      Nat. Struct. Biol. 3:856-862(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
    13. "The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold."
      Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H., Qamar S., Plater A., Berry A., Hunter W.N.
      Structure 4:1303-1315(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
    14. "The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity."
      Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.
      J. Mol. Biol. 287:383-394(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG, ACTIVE SITE.
    15. "The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase."
      Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N.
      Acta Crystallogr. D 59:611-614(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, METAL BINDING SITES.

    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: July 22, 2015
    This is version 90 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

    External Data

    Dasty 3

    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 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.