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P0A870 (TALB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transaldolase B

EC=2.2.1.2
Gene names
Name:talB
Synonyms:yaaK
Ordered Locus Names:b0008, JW0007
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

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. Ref.1

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. HAMAP-Rule MF_00492

Subunit structure

Homodimer. Ref.1 Ref.9

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00492.

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=38 µM for D,L-glyceraldehyde 3-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius) Ref.1

KM=90 µM for D-erythrose-4-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)

KM=31 mM for D-ribose-5-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)

KM=28 mM for D-glyceraldehyde (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)

KM=285 µM for D-sedoheptulose-7-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)

KM=1200 µM for D-fructose-6-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)

pH dependence:

Optimum pH is between 8.5 and 9.5.

Temperature dependence:

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.

Ontologies

Keywords
   Biological processPentose shunt
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionsedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.6 Ref.7
Chain2 – 317316Transaldolase B HAMAP-Rule MF_00492
PRO_0000173593

Sites

Active site1321Schiff-base intermediate with substrate Ref.11

Secondary structure

.................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A870 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2DF03D741E576C31

FASTA31735,219
        10         20         30         40         50         60 
MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK 

        70         80         90        100        110        120 
QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN 

       130        140        150        160        170        180 
DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG 

       190        200        210        220        230        240 
RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD 

       250        260        270        280        290        300 
RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR 

       310 
KFAIDQEKLE KMIGDLL 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
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).

Web resources

Wikipedia

Transaldolase B entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13161 Genomic DNA. Translation: BAA21822.1.
S80045 Genomic DNA. Translation: AAB47022.1.
U00096 Genomic DNA. Translation: AAC73119.1.
AP009048 Genomic DNA. Translation: BAB96586.1.
PIRS40535.
RefSeqNP_414549.1. NC_000913.3.
YP_488314.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A870.
SMRP0A870. Positions 2-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31850N.
IntActP0A870. 6 interactions.
STRING511145.b0008.

PTM databases

PhosSiteP0810439.

2D gel databases

SWISS-2DPAGEP0A870.

Proteomic databases

PaxDbP0A870.
PRIDEP0A870.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73119; AAC73119; b0008.
BAB96586; BAB96586; BAB96586.
GeneID12932945.
944748.
KEGGecj:Y75_p0008.
eco:b0008.
PATRIC32115111. VBIEscCol129921_0007.

Organism-specific databases

EchoBASEEB1517.
EcoGeneEG11556. talB.

Phylogenomic databases

eggNOGCOG0176.
HOGENOMHOG000281234.
KOK00616.
OMAAQMPAYQ.
OrthoDBEOG6G7R4D.
ProtClustDBPRK05269.

Enzyme and pathway databases

BioCycECOL316407:JW0007-MONOMER.
UniPathwayUPA00115; UER00414.

Gene expression databases

GenevestigatorP0A870.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00492. Transaldolase_1.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00874. talAB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A870.
PROP0A870.

Entry information

Entry nameTALB_ECOLI
AccessionPrimary (citable) accession number: P0A870
Secondary accession number(s): P30148
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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