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InterPro: IPR004730 Transaldolase AB

Protein matches Help

UniProtKB

Matches:

830 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004730 Transaldolase_AB

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR10683:SF3	Transaldolase_AB	821
TIGRFAMs	TIGR00874	talAB	771
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001585 Transaldolase

Contains

IPR013785 Aldolase-type TIM barrel
IPR018225 Transaldolase, active site

GO Term annotation Help

Process

GO:0006098 pentose-phosphate shunt

Function

GO:0004801 transaldolase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Transaldolase (EC:2.2.1.2) catalyzes the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways. Transaldolase is an enzyme of about 34 Kd whose sequence has been well conserved throughout evolution. A lysine has been implicated [1] in the catalytic mechanism of the enzyme; it acts as a nucleophilic group that attacks the carbonyl group of fructose-6-phosphate.

Transaldolase is evolutionary related [2] to a bacterial protein of about 20 Kd (known as talC in Escherichia coli), whose exact function is not yet known.

Structural links Help

PDB - click here

SCOP: c.1.10.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:2.2.1.2

CluSTr: ALLvsALL:5278:51.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004730

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P37837 Transaldolase

P53228 Transaldolase NQM1

P72797 Transaldolase

Q93092 Transaldolase

Q9W1G0 Probable transaldolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR002048	Calcium-binding EF-hand
IPR018225	Transaldolase, active site
IPR001585	Transaldolase
IPR004730	Transaldolase AB
IPR018247	EF-Hand 1, calcium-binding site
IPR018249	EF-HAND 2
IPR018248	EF-Hand domain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Miosga T, Schaaff-Gerstenschlager I, Franken E, Zimmermann FK. Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Yeast 9 1241-9 1993 [PubMed: 8109173] http://dx.doi.org/10.1002/yea.320091111
2.	Reizer J, Reizer A, Saier MH Jr. Novel phosphotransferase system genes revealed by bacterial genome analysis--a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system. Microbiology (Reading, Engl.) 141 ( Pt 4) 961-71 1995 [PubMed: 7773398]

Additional Reading Open in usermanual
	Schorken U, Thorell S, Schurmann M, Jia J, Sprenger GA, Schneider G. Identification of catalytically important residues in the active site of Escherichia coli transaldolase. Eur. J. Biochem. 268 2001 2408-15 [PubMed: 11298760] http://dx.doi.org/10.1046/j.1432-1327.2001.02128.x
	Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G. The three-dimensional structure of human transaldolase. FEBS Lett. 475 2000 205-8 [PubMed: 10869557] http://dx.doi.org/10.1016/S0014-5793(00)01658-6
	Jia J, Schorken U, Lindqvist Y, Sprenger GA, Schneider G. Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases. Protein Sci. 6 1997 119-24 [PubMed: 9007983] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9007983
	Jia J, Huang W, Schorken U, Sahm H, Sprenger GA, Lindqvist Y, Schneider G. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family. Structure 4 1996 715-24 [PubMed: 8805555] http://dx.doi.org/10.1016/S0969-2126(96)00077-9

InterPro 23.1