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Protein

Fructose-6-phosphate aldolase 2

Gene

fsaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize hydroxyacetone as an alternative donor substrate. Is also able to catalyze the direct self-aldol addition of glycolaldehyde. Is less catalytically efficient than the isozyme FsaA. Does not display transaldolase activity.2 Publications

Catalytic activityi

D-fructose 6-phosphate = glycerone + D-glyceraldehyde 3-phosphate.2 Publications

Kineticsi

Catalytic efficiency is 28-fold higher using glyceraldehyde 3-phosphate as acceptor substrate and hydroxyacetone as donor substrate than with dihydroxyacetone as the donor.

  1. KM=27 mM for dihydroxyacetone1 Publication
  2. KM=15 mM for hydroxyacetone1 Publication
  3. KM=0.28 mM for glycolaldehyde (as donor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  4. KM=65 mM for glycolaldehyde (as acceptor substrate in the self-aldol addition of glycolaldehyde)1 Publication
  5. KM=0.65 mM for D,L-glyceraldehyde 3-phosphate1 Publication
  6. KM=6.70 mM for D-fructose 6-phosphate1 Publication
  7. KM=210 mM for D-fructose1 Publication
  8. KM=271 mM for D-sorbose1 Publication

    pH dependencei

    Optimum pH is 8.5 for the retroaldol activity on F6P.1 Publication

    Temperature dependencei

    Is not thermally stable at temperatures higher than 60 degrees Celsius. Is less thermostable than the isozyme FsaA.1 Publication

    Sites

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

    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:EG11905-MONOMER.
    ECOL316407:JW3918-MONOMER.
    MetaCyc:EG11905-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-6-phosphate aldolase 2 (EC:4.1.2.-)
    Alternative name(s):
    Fructose-6-phosphate aldolase B
    Short name:
    FSAB
    Gene namesi
    Name:fsaB
    Synonyms:talC, yijG
    Ordered Locus Names:b3946, JW3918
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11905. fsaB.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Fructose-6-phosphate aldolase 2PRO_0000173646Add
    BLAST

    Proteomic databases

    PaxDbiP32669.

    Interactioni

    Subunit structurei

    Homodecamer.1 Publication

    Protein-protein interaction databases

    BioGridi4263139. 10 interactions.
    IntActiP32669. 5 interactions.
    STRINGi511145.b3946.

    Structurei

    3D structure databases

    ProteinModelPortaliP32669.
    SMRiP32669. Positions 1-220.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4107T9Z. Bacteria.
    COG0176. LUCA.
    HOGENOMiHOG000226075.
    InParanoidiP32669.
    KOiK08314.
    OMAiQMLGTPA.
    OrthoDBiEOG6PS600.
    PhylomeDBiP32669.

    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.

    P32669-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MELYLDTANV AEVERLARIF PIAGVTTNPS IIAASKESIW EVLPRLQKAI
    60 70 80 90 100
    GDEGILFAQT MSRDAQGMVE EAKRLRDAIP GIVVKIPVTS EGLAAIKILK
    110 120 130 140 150
    KEGITTLGTA VYSAAQGLLA ALAGAKYVAP YVNRVDAQGG DGIRTVQELQ
    160 170 180 190 200
    TLLEMHAPES MVLAASFKTP RQALDCLLAG CESITLPLDV AQQMLNTPAV
    210 220
    ESAIEKFEHD WNAAFGTTHL
    Length:220
    Mass (Da):23,555
    Last modified:October 1, 1993 - v1
    Checksum:i95D72DFD475BDE7B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00006 Genomic DNA. Translation: AAC43052.1.
    U00096 Genomic DNA. Translation: AAC76928.1.
    AP009048 Genomic DNA. Translation: BAE77364.1.
    PIRiE65201.
    RefSeqiNP_418381.1. NC_000913.3.
    WP_000424840.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76928; AAC76928; b3946.
    BAE77364; BAE77364; BAE77364.
    GeneIDi948439.
    KEGGiecj:JW3918.
    eco:b3946.
    PATRICi32123415. VBIEscCol129921_4068.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00006 Genomic DNA. Translation: AAC43052.1.
    U00096 Genomic DNA. Translation: AAC76928.1.
    AP009048 Genomic DNA. Translation: BAE77364.1.
    PIRiE65201.
    RefSeqiNP_418381.1. NC_000913.3.
    WP_000424840.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP32669.
    SMRiP32669. Positions 1-220.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263139. 10 interactions.
    IntActiP32669. 5 interactions.
    STRINGi511145.b3946.

    Proteomic databases

    PaxDbiP32669.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76928; AAC76928; b3946.
    BAE77364; BAE77364; BAE77364.
    GeneIDi948439.
    KEGGiecj:JW3918.
    eco:b3946.
    PATRICi32123415. VBIEscCol129921_4068.

    Organism-specific databases

    EchoBASEiEB1850.
    EcoGeneiEG11905. fsaB.

    Phylogenomic databases

    eggNOGiENOG4107T9Z. Bacteria.
    COG0176. LUCA.
    HOGENOMiHOG000226075.
    InParanoidiP32669.
    KOiK08314.
    OMAiQMLGTPA.
    OrthoDBiEOG6PS600.
    PhylomeDBiP32669.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11905-MONOMER.
    ECOL316407:JW3918-MONOMER.
    MetaCyc:EG11905-MONOMER.

    Miscellaneous databases

    PROiP32669.

    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. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Novel phosphotransferase system genes revealed by bacterial genome analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system."
      Reizer J., Reizer A., Saier M.H. Jr.
      Microbiology 141:961-971(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISCUSSION OF SEQUENCE.
    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: FUNCTION, CATALYTIC ACTIVITY.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    6. "FSAB: A new fructose-6-phosphate aldolase from Escherichia coli. Cloning, over-expression and comparative kinetic characterization with FSAA."
      Sanchez-Moreno I., Nauton L., Thery V., Pinet A., Petit J.-L., de Berardinis V., Samland A.K., Guerard-Helaine C., Lemaire M.
      J. Mol. Catal., B Enzym. 84:9-14(2012)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, 3D-STRUCTURE MODELING.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

    Entry informationi

    Entry nameiFSAB_ECOLI
    AccessioniPrimary (citable) accession number: P32669
    Secondary accession number(s): Q2M8P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: January 20, 2016
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. 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.