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Protein

Transaldolase B

Gene

talB

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

Functioni

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.1 Publication

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.1 Publication

Enzyme regulationi

Inhibited by Tris-HCl and phosphate buffer. Also competitively inhibited by sugars with L configuration at C2, such as D-arabinose-5-phosphate and L-glyceraldehyde.1 Publication

Kineticsi

  1. KM=38 µM for D,L-glyceraldehyde 3-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)1 Publication
  2. KM=90 µM for D-erythrose-4-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)1 Publication
  3. KM=31 mM for D-ribose-5-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)1 Publication
  4. KM=28 mM for D-glyceraldehyde (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)1 Publication
  5. KM=285 µM for D-sedoheptulose-7-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)1 Publication
  6. KM=1200 µM for D-fructose-6-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is between 8.5 and 9.5.1 Publication

    Temperature dependencei

    Optimum temperature is between 15 and 40 degrees Celsius. At temperatures above 50 degrees Celsius, activity is lost rapidly, and at 55 degrees Celsius, the enzyme is totally inactivated.1 Publication

    Pathwayi: pentose phosphate pathway

    This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage).
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Transaldolase B (talB), Transaldolase A (talA)
    3. no protein annotated in this organism
    This subpathway is part of the pathway pentose phosphate pathway, 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 beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei132 – 1321Schiff-base intermediate with substrate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Pentose shunt

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciECOL316407:JW0007-MONOMER.
    BRENDAi2.2.1.2. 2026.
    UniPathwayiUPA00115; UER00414.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transaldolase B (EC:2.2.1.2)
    Gene namesi
    Name:talB
    Synonyms:yaaK
    Ordered Locus Names:b0008, JW0007
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11556. talB.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved3 Publications
    Chaini2 – 317316Transaldolase BPRO_0000173593Add
    BLAST

    Proteomic databases

    PaxDbiP0A870.
    PRIDEiP0A870.

    2D gel databases

    SWISS-2DPAGEP0A870.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi4261939. 3 interactions.
    DIPiDIP-31850N.
    IntActiP0A870. 6 interactions.
    STRINGi511145.b0008.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 96Combined sources
    Beta strandi12 – 176Combined sources
    Helixi21 – 277Combined sources
    Beta strandi30 – 334Combined sources
    Helixi36 – 427Combined sources
    Helixi46 – 483Combined sources
    Helixi49 – 6214Combined sources
    Helixi66 – 8621Combined sources
    Beta strandi93 – 964Combined sources
    Helixi99 – 1013Combined sources
    Helixi105 – 12117Combined sources
    Helixi126 – 1283Combined sources
    Beta strandi129 – 1346Combined sources
    Helixi137 – 14812Combined sources
    Beta strandi153 – 1586Combined sources
    Helixi161 – 1699Combined sources
    Beta strandi173 – 1797Combined sources
    Helixi180 – 18910Combined sources
    Helixi197 – 1993Combined sources
    Helixi201 – 21515Combined sources
    Beta strandi221 – 2255Combined sources
    Helixi230 – 2345Combined sources
    Turni235 – 2384Combined sources
    Beta strandi239 – 2446Combined sources
    Helixi246 – 2538Combined sources
    Beta strandi255 – 2573Combined sources
    Helixi278 – 2869Combined sources
    Helixi289 – 31426Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I2NX-ray2.05A/B2-317[»]
    1I2OX-ray2.05A/B2-317[»]
    1I2PX-ray2.05A/B2-317[»]
    1I2QX-ray2.05A/B2-317[»]
    1I2RX-ray2.10A/B2-317[»]
    1ONRX-ray1.87A/B2-317[»]
    1UCWX-ray2.20A/B1-317[»]
    3KOFX-ray1.90A/B1-317[»]
    4RZ5X-ray1.80A/B1-317[»]
    4RZ6X-ray1.80A/B1-317[»]
    ProteinModelPortaliP0A870.
    SMRiP0A870. Positions 2-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A870.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transaldolase family. Type 1 subfamily.Curated

    Phylogenomic databases

    eggNOGiENOG4105CW3. Bacteria.
    COG0176. LUCA.
    HOGENOMiHOG000281234.
    InParanoidiP0A870.
    KOiK00616.
    OMAiEYAGNED.
    OrthoDBiEOG6G7R4D.
    PhylomeDBiP0A870.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00492. Transaldolase_1.
    InterProiIPR013785. Aldolase_TIM.
    IPR001585. TAL/FSA.
    IPR004730. Transaldolase_1.
    IPR018225. Transaldolase_AS.
    [Graphical view]
    PANTHERiPTHR10683. PTHR10683. 1 hit.
    PfamiPF00923. Transaldolase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00874. talAB. 1 hit.
    PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
    PS00958. TRANSALDOLASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A870-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK
    60 70 80 90 100
    LIDDAVAWAK QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR
    110 120 130 140 150
    LSYDTEASIA KAKRLIKLYN DAGISNDRIL IKLASTWQGI RAAEQLEKEG
    160 170 180 190 200
    INCNLTLLFS FAQARACAEA GVFLISPFVG RILDWYKANT DKKEYAPAED
    210 220 230 240 250
    PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD RLTIAPALLK
    260 270 280 290 300
    ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
    310
    KFAIDQEKLE KMIGDLL
    Length:317
    Mass (Da):35,219
    Last modified:January 23, 2007 - v2
    Checksum:i2DF03D741E576C31
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D13161 Genomic DNA. Translation: BAA21822.1.
    S80045 Genomic DNA. Translation: AAB47022.1.
    U00096 Genomic DNA. Translation: AAC73119.1.
    AP009048 Genomic DNA. Translation: BAB96586.1.
    PIRiS40535.
    RefSeqiNP_414549.1. NC_000913.3.
    WP_000130185.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73119; AAC73119; b0008.
    BAB96586; BAB96586; BAB96586.
    GeneIDi944748.
    KEGGiecj:JW0007.
    eco:b0008.
    PATRICi32115111. VBIEscCol129921_0007.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Transaldolase B entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D13161 Genomic DNA. Translation: BAA21822.1.
    S80045 Genomic DNA. Translation: AAB47022.1.
    U00096 Genomic DNA. Translation: AAC73119.1.
    AP009048 Genomic DNA. Translation: BAB96586.1.
    PIRiS40535.
    RefSeqiNP_414549.1. NC_000913.3.
    WP_000130185.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I2NX-ray2.05A/B2-317[»]
    1I2OX-ray2.05A/B2-317[»]
    1I2PX-ray2.05A/B2-317[»]
    1I2QX-ray2.05A/B2-317[»]
    1I2RX-ray2.10A/B2-317[»]
    1ONRX-ray1.87A/B2-317[»]
    1UCWX-ray2.20A/B1-317[»]
    3KOFX-ray1.90A/B1-317[»]
    4RZ5X-ray1.80A/B1-317[»]
    4RZ6X-ray1.80A/B1-317[»]
    ProteinModelPortaliP0A870.
    SMRiP0A870. Positions 2-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261939. 3 interactions.
    DIPiDIP-31850N.
    IntActiP0A870. 6 interactions.
    STRINGi511145.b0008.

    2D gel databases

    SWISS-2DPAGEP0A870.

    Proteomic databases

    PaxDbiP0A870.
    PRIDEiP0A870.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73119; AAC73119; b0008.
    BAB96586; BAB96586; BAB96586.
    GeneIDi944748.
    KEGGiecj:JW0007.
    eco:b0008.
    PATRICi32115111. VBIEscCol129921_0007.

    Organism-specific databases

    EchoBASEiEB1517.
    EcoGeneiEG11556. talB.

    Phylogenomic databases

    eggNOGiENOG4105CW3. Bacteria.
    COG0176. LUCA.
    HOGENOMiHOG000281234.
    InParanoidiP0A870.
    KOiK00616.
    OMAiEYAGNED.
    OrthoDBiEOG6G7R4D.
    PhylomeDBiP0A870.

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00414.
    BioCyciECOL316407:JW0007-MONOMER.
    BRENDAi2.2.1.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A870.
    PROiP0A870.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00492. Transaldolase_1.
    InterProiIPR013785. Aldolase_TIM.
    IPR001585. TAL/FSA.
    IPR004730. Transaldolase_1.
    IPR018225. Transaldolase_AS.
    [Graphical view]
    PANTHERiPTHR10683. PTHR10683. 1 hit.
    PfamiPF00923. Transaldolase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00874. talAB. 1 hit.
    PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
    PS00958. TRANSALDOLASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
      Sprenger G.A., Schorken U., Sprenger G., Sahm H.
      J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
    2. Iida A., Teshiba S., Mizobuchi K.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "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.
    8. Sprenger G.A.
      Unpublished observations (JUN-1993)
      Cited for: PRESENCE OF TWO TRANSALDOLASES IN E.COLI.
    9. "Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family."
      Jia J., Huang W., Schoerken U., Sham H., Sprenger G.A., Lindqvist Y., Schneider G.
      Structure 4:715-724(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS), SUBUNIT.
    10. "Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases."
      Jia J., Schorken U., Lindqvist Y., Sprenger G.A., Schneider G.
      Protein Sci. 6:119-124(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    11. "Identification of catalytically important residues in the active site of Escherichia coli transaldolase."
      Schorken U., Thorell S., Schurmann M., Jia J., Sprenger G.A., Schneider G.
      Eur. J. Biochem. 268:2408-2415(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), ACTIVE SITE.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    12. "Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards nonphosphorylated substrates."
      Schneider S., Gutierrez M., Sandalova T., Schneider G., Clapes P., Sprenger G.A., Samland A.K.
      ChemBioChem 11:681-690(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiTALB_ECOLI
    AccessioniPrimary (citable) accession number: P0A870
    Secondary accession number(s): P30148
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: January 20, 2016
    This is version 109 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.