EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR015941 Transketolase-like, C-terminal

Protein matches Help

UniProtKB

Matches:

9158 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

IPR015941 Transketolase-like_C

Secondary

IPR009014

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.920	Transketo_C_like	9158
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009014 Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II

Children

IPR005476 Transketolase, C-terminal

Found in

IPR004660 2-oxo-acid dehydrogenase E1 component homodimeric type
IPR011895 Pyruvate-flavodoxin oxidoreductase
IPR017600 Alpha-ketoglutarate dehydrogenase

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

Transketolase C-terminal-like domains [1] can be found in a number of different enzymes, including the C-terminal domain of the pyruvate dehydrogenase E1 component [2], the C-terminal domain of branched-chain alpha-keto acid dehydrogenases [3], and domain II of pyruvate-ferredoxin oxidoreductase (PFOR) [4]. Structural studies reveal this domain to comprise of three layers alpha/beta/alpha. The mixed beta sheet consists of five strands in the order 13245, where strand 1 is antiparallel to the others.

Structural links Help

PDB - click here

SCOP: c.48.1.1 , c.48.1.2 , c.48.1.3

CATH: 3.40.50.920

Database links Help

Enzyme: EC:2.2.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015941

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O44451 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

P23254 Transketolase 1

P40142 Transketolase

Q38799 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

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 Open in usermanual
1.	Nikkola M, Lindqvist Y, Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution. J. Mol. Biol. 238 387-404 1994 [PubMed: 8176731] http://dx.doi.org/10.1006/jmbi.1994.1299
2.	Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 41 5213-21 2002 [PubMed: 11955070] http://dx.doi.org/10.1021/bi0118557
3.	Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 6 785-92 1999 [PubMed: 10426958] http://dx.doi.org/10.1038/11563
4.	Chabriere E, Vernede X, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC. Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase. Science 294 2559-63 2001 [PubMed: 11752578] http://dx.doi.org/10.1126/science.1066198

Additional Reading Open in usermanual
	Kale S, Arjunan P, Furey W, Jordan F. A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J. Biol. Chem. 282 2007 28106-16 [PubMed: 17635929] http://dx.doi.org/10.1074/jbc.M704326200
	Seifert F, Ciszak E, Korotchkina L, Golbik R, Spinka M, Dominiak P, Sidhu S, Brauer J, Patel MS, Tittmann K. Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex. Biochemistry 46 2007 6277-87 [PubMed: 17474719] http://dx.doi.org/10.1021/bi700083z
	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
	Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC. Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate. Structure 14 2006 217-24 [PubMed: 16472741] http://dx.doi.org/10.1016/j.str.2005.10.013
	Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT. A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. Structure 14 2006 287-98 [PubMed: 16472748] http://dx.doi.org/10.1016/j.str.2005.10.009

InterPro 23.1