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Protein

Transaldolase B

Gene

talB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Activity 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 A (talA), Transaldolase B (talB)
    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)DescriptionActionsGraphical viewLength
    Active sitei132Schiff-base intermediate with substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processPentose shunt
    LigandSchiff base

    Enzyme and pathway databases

    BioCyciEcoCyc:TRANSALDOLB-MONOMER
    MetaCyc:TRANSALDOLB-MONOMER
    BRENDAi2.2.1.2 2026
    UniPathwayi
    UPA00115;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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11556 talB

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • intracellular Source: GO_Central
    • membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved3 Publications
    ChainiPRO_00001735932 – 317Transaldolase BAdd BLAST316

    Proteomic databases

    EPDiP0A870
    PaxDbiP0A870
    PRIDEiP0A870

    2D gel databases

    SWISS-2DPAGEiP0A870

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi4261939, 9 interactors
    DIPiDIP-31850N
    IntActiP0A870, 9 interactors
    STRINGi316385.ECDH10B_0008

    Structurei

    Secondary structure

    1317
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP0A870
    SMRiP0A870
    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
    PhylomeDBiP0A870

    Family and domain databases

    CDDicd00957 Transaldolase_TalAB, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_00492 Transaldolase_1, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR001585 TAL/FSA
    IPR004730 Transaldolase_1
    IPR018225 Transaldolase_AS
    PANTHERiPTHR10683 PTHR10683, 1 hit
    PTHR10683:SF20 PTHR10683:SF20, 1 hit
    PfamiView protein in Pfam
    PF00923 TAL_FSA, 1 hit
    TIGRFAMsiTIGR00874 talAB, 1 hit
    PROSITEiView protein in PROSITE
    PS01054 TRANSALDOLASE_1, 1 hit
    PS00958 TRANSALDOLASE_2, 1 hit

    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
    PATRICifig|1411691.4.peg.2275

    Similar proteinsi

    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
    PDB 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[»]
    4S2BX-ray1.46A/B1-317[»]
    4S2CX-ray2.20A/B1-317[»]
    ProteinModelPortaliP0A870
    SMRiP0A870
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261939, 9 interactors
    DIPiDIP-31850N
    IntActiP0A870, 9 interactors
    STRINGi316385.ECDH10B_0008

    2D gel databases

    SWISS-2DPAGEiP0A870

    Proteomic databases

    EPDiP0A870
    PaxDbiP0A870
    PRIDEiP0A870

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73119; AAC73119; b0008
    BAB96586; BAB96586; BAB96586
    GeneIDi944748
    KEGGiecj:JW0007
    eco:b0008
    PATRICifig|1411691.4.peg.2275

    Organism-specific databases

    EchoBASEiEB1517
    EcoGeneiEG11556 talB

    Phylogenomic databases

    eggNOGiENOG4105CW3 Bacteria
    COG0176 LUCA
    HOGENOMiHOG000281234
    InParanoidiP0A870
    KOiK00616
    PhylomeDBiP0A870

    Enzyme and pathway databases

    UniPathwayi
    UPA00115;UER00414

    BioCyciEcoCyc:TRANSALDOLB-MONOMER
    MetaCyc:TRANSALDOLB-MONOMER
    BRENDAi2.2.1.2 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A870
    PROiPR:P0A870

    Family and domain databases

    CDDicd00957 Transaldolase_TalAB, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_00492 Transaldolase_1, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR001585 TAL/FSA
    IPR004730 Transaldolase_1
    IPR018225 Transaldolase_AS
    PANTHERiPTHR10683 PTHR10683, 1 hit
    PTHR10683:SF20 PTHR10683:SF20, 1 hit
    PfamiView protein in Pfam
    PF00923 TAL_FSA, 1 hit
    TIGRFAMsiTIGR00874 talAB, 1 hit
    PROSITEiView protein in PROSITE
    PS01054 TRANSALDOLASE_1, 1 hit
    PS00958 TRANSALDOLASE_2, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTALB_ECOLI
    AccessioniPrimary (citable) accession number: P0A870
    Secondary accession number(s): P30148
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: November 7, 2018
    This is version 126 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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