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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

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. carbohydrate metabolic process Source: InterPro
  2. pentose-phosphate shunt Source: UniProtKB-HAMAP
Complete GO annotation...

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
Complete GO annotation...

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.

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 – 85Combined sources
Turni9 – 113Combined sources
Beta strandi12 – 198Combined 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 – 1889Combined sources
Beta strandi189 – 1913Combined sources
Helixi197 – 1993Combined sources
Helixi201 – 21515Combined sources
Beta strandi221 – 2255Combined sources
Helixi230 – 2356Combined sources
Turni236 – 2383Combined sources
Beta strandi239 – 2446Combined sources
Helixi246 – 2549Combined 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[»]
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

eggNOGiCOG0176.
HOGENOMiHOG000281234.
InParanoidiP0A870.
KOiK00616.
OMAiFNAIDEY.
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

        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.
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:
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.
YP_488314.1. NC_007779.1.

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[»]
ProteinModelPortaliP0A870.
SMRiP0A870. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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.
GeneIDi12932945.
944748.
KEGGiecj:Y75_p0008.
eco:b0008.
PATRICi32115111. VBIEscCol129921_0007.

Organism-specific databases

EchoBASEiEB1517.
EcoGeneiEG11556. talB.

Phylogenomic databases

eggNOGiCOG0176.
HOGENOMiHOG000281234.
InParanoidiP0A870.
KOiK00616.
OMAiFNAIDEY.
OrthoDBiEOG6G7R4D.
PhylomeDBiP0A870.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00414.
BioCyciECOL316407:JW0007-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A870.
PROiP0A870.

Gene expression databases

GenevestigatoriP0A870.

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]
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: March 4, 2015
This is version 100 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

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 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.