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P0A870

- TALB_ECOLI

UniProt

P0A870 - TALB_ECOLI

Protein

Transaldolase B

Gene

talB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Sites

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

    GO - Molecular functioni

    1. sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Source: UniProtKB

    GO - Biological processi

    1. pentose-phosphate shunt Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Pentose shunt

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciECOL316407:JW0007-MONOMER.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11556. talB.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 317316Transaldolase BPRO_0000173593Add
    BLAST

    Proteomic databases

    PaxDbiP0A870.
    PRIDEiP0A870.

    2D gel databases

    SWISS-2DPAGEP0A870.

    PTM databases

    PhosSiteiP0810439.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A870.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    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 – 85
    Turni9 – 113
    Beta strandi12 – 198
    Helixi21 – 277
    Beta strandi30 – 334
    Helixi36 – 427
    Helixi46 – 483
    Helixi49 – 6214
    Helixi66 – 8621
    Beta strandi93 – 964
    Helixi99 – 1013
    Helixi105 – 12117
    Helixi126 – 1283
    Beta strandi129 – 1346
    Helixi137 – 14812
    Beta strandi153 – 1586
    Helixi161 – 1699
    Beta strandi173 – 1797
    Helixi180 – 1889
    Beta strandi189 – 1913
    Helixi197 – 1993
    Helixi201 – 21515
    Beta strandi221 – 2255
    Helixi230 – 2356
    Turni236 – 2383
    Beta strandi239 – 2446
    Helixi246 – 2549
    Beta strandi255 – 2573
    Helixi278 – 2869
    Helixi289 – 31426

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP0A870.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A870.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transaldolase family. Type 1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0176.
    HOGENOMiHOG000281234.
    KOiK00616.
    OMAiSYEPHED.
    OrthoDBiEOG6G7R4D.
    PhylomeDBiP0A870.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00492. Transaldolase_1.
    InterProiIPR013785. Aldolase_TIM.
    IPR001585. Transaldolase.
    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

    MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK    50
    LIDDAVAWAK QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR 100
    LSYDTEASIA KAKRLIKLYN DAGISNDRIL IKLASTWQGI RAAEQLEKEG 150
    INCNLTLLFS FAQARACAEA GVFLISPFVG RILDWYKANT DKKEYAPAED 200
    PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD RLTIAPALLK 250
    ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR 300
    KFAIDQEKLE KMIGDLL 317
    Length:317
    Mass (Da):35,219
    Last modified:January 23, 2007 - v2
    Checksum:i2DF03D741E576C31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488314.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73119; AAC73119; b0008.
    BAB96586; BAB96586; BAB96586.
    GeneIDi12932945.
    944748.
    KEGGiecj:Y75_p0008.
    eco:b0008.
    PATRICi32115111. VBIEscCol129921_0007.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Transaldolase B entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S40535.
    RefSeqi NP_414549.1. NC_000913.3.
    YP_488314.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I2N X-ray 2.05 A/B 2-317 [» ]
    1I2O X-ray 2.05 A/B 2-317 [» ]
    1I2P X-ray 2.05 A/B 2-317 [» ]
    1I2Q X-ray 2.05 A/B 2-317 [» ]
    1I2R X-ray 2.10 A/B 2-317 [» ]
    1ONR X-ray 1.87 A/B 2-317 [» ]
    1UCW X-ray 2.20 A/B 1-317 [» ]
    3KOF X-ray 1.90 A/B 1-317 [» ]
    ProteinModelPortali P0A870.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31850N.
    IntActi P0A870. 6 interactions.
    STRINGi 511145.b0008.

    PTM databases

    PhosSitei P0810439.

    2D gel databases

    SWISS-2DPAGE P0A870.

    Proteomic databases

    PaxDbi P0A870.
    PRIDEi P0A870.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73119 ; AAC73119 ; b0008 .
    BAB96586 ; BAB96586 ; BAB96586 .
    GeneIDi 12932945.
    944748.
    KEGGi ecj:Y75_p0008.
    eco:b0008.
    PATRICi 32115111. VBIEscCol129921_0007.

    Organism-specific databases

    EchoBASEi EB1517.
    EcoGenei EG11556. talB.

    Phylogenomic databases

    eggNOGi COG0176.
    HOGENOMi HOG000281234.
    KOi K00616.
    OMAi SYEPHED.
    OrthoDBi EOG6G7R4D.
    PhylomeDBi P0A870.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00414 .
    BioCyci ECOL316407:JW0007-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A870.
    PROi P0A870.

    Gene expression databases

    Genevestigatori P0A870.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00492. Transaldolase_1.
    InterProi IPR013785. Aldolase_TIM.
    IPR001585. Transaldolase.
    IPR004730. Transaldolase_1.
    IPR018225. Transaldolase_AS.
    [Graphical view ]
    PANTHERi PTHR10683. PTHR10683. 1 hit.
    Pfami PF00923. Transaldolase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00874. talAB. 1 hit.
    PROSITEi PS01054. TRANSALDOLASE_1. 1 hit.
    PS00958. TRANSALDOLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 96 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