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InterPro: IPR005478 Transketolase, bacterial-like

Protein matches Help

UniProtKB

Matches:

2282 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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

IPR005478 Transketolase_bac-like

Secondary

IPR000360

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11624:SF1	BacTransketolase	2267
TIGRFAMs	TIGR00232	tktlase_bact	1882
Signatures in BioMart

InterPro Relationships Help

Contains

IPR005474 Transketolase, N-terminal
IPR005475 Transketolase-like, pyrimidine-binding domain
IPR005476 Transketolase, C-terminal
IPR020826 Transketolase binding site

GO Term annotation Help

Function

GO:0004802 transketolase activity

InterPro annotation

Entry Details in BioMart

Abstract

Transketolase (EC:2.2.1.1) (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor.

This group includes two proteins from the yeast Saccharomyces cerevisiae (Baker's yeast) but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous.

Structural links Help

PDB - click here

SCOP: c.36.1.10 , c.36.1.6 , c.48.1.1

CATH: 3.40.50.920 , 3.40.50.970

Database links Help

Enzyme: EC:2.2.1.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005478

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O93884 Dihydroxyacetone synthase

P23254 Transketolase 1

P27302 Transketolase 1

Q7SIC9 Transketolase, chloroplastic

Q8YRU9 Transketolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020826	Transketolase binding site
IPR005474	Transketolase, N-terminal
IPR009014	Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II
IPR005476	Transketolase, C-terminal
IPR005475	Transketolase-like, pyrimidine-binding domain
IPR005478	Transketolase, bacterial-like
IPR015941	Transketolase-like, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Fiedler E, Thorell S, Sandalova T, Golbik R, Konig S, Schneider G. Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 99 2002 591-5 [PubMed: 11773632] http://dx.doi.org/10.1073/pnas.022510999
	Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G. Identification of catalytically important residues in yeast transketolase. Biochemistry 36 1997 15643-9 [PubMed: 9398292] http://dx.doi.org/10.1021/bi971606b
	Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M. Structure and properties of an engineered transketolase from maize. Plant Physiol. 132 2003 1941-9 [PubMed: 12913150] http://dx.doi.org/10.1104/pp.103.020982
	Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP. Transketolase from Leishmania mexicana has a dual subcellular localization. Biochem. J. 382 2004 759-67 [PubMed: 15149284] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=15149284
	Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G, Tittmann K. Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46 2007 12037-52 [PubMed: 17914867] http://dx.doi.org/10.1021/bi700844m

InterPro 23.1