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InterPro: IPR004731 Transaldolase C

Protein matches Help

UniProtKB

Matches:

843 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

IPR004731 Transaldolase_C

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00875	talC	843
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:0005975 carbohydrate metabolic process

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:43431:40.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004731

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A4FWM6 Probable transaldolase

P78055 Fructose-6-phosphate aldolase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018225	Transaldolase, active site
IPR013785	Aldolase-type TIM barrel
IPR001585	Transaldolase
IPR004731	Transaldolase C
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH 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
	Thorell S, Schurmann M, Sprenger GA, Schneider G. Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family. J. Mol. Biol. 319 2002 161-71 [PubMed: 12051943] http://dx.doi.org/10.1016/S0022-2836(02)00258-9

InterPro 23.1