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P0A870

- TALB_ECOLI

UniProt

P0A870 - TALB_ECOLI

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Protein
Transaldolase B
Gene
talB, yaaK, b0008, JW0007
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)
  3. KM=31 mM for D-ribose-5-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
  4. KM=28 mM for D-glyceraldehyde (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
  5. KM=285 µM for D-sedoheptulose-7-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)
  6. KM=1200 µM for D-fructose-6-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)

pH dependencei

Optimum pH is between 8.5 and 9.5.

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.

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
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 Inferred UniRule annotation

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 BUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP0A870.

Family & Domainsi

Sequence similaritiesi

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

« 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: July 9, 2014
This is version 95 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

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