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InterPro: IPR011766 Thiamine pyrophosphate enzyme, C-terminal TPP-binding

Protein matches Help

UniProtKB

Matches:

8614 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

IPR011766 TPP_enzyme_bd_C

Secondary

IPR000399

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02775	TPP_enzyme_C	8614
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006397 Glyoxylate carboligase
IPR011895 Pyruvate-flavodoxin oxidoreductase
IPR011896 2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate
IPR012782 Acetolactate synthase, catabolic
IPR012846 Acetolactate synthase, large subunit, biosynthetic
IPR014092 Pyruvate oxidase
IPR017660 Oxalyl-CoA decarboxylase
IPR017684 Phosphonopyruvate decarboxylase
IPR017721 Indolepyruvate ferredoxin oxidoreductase, alpha subunit
IPR017764 Indolepyruvate decarboxylase
IPR017765 Indolepyruvate/phenylpyruvate decarboxylase
IPR017820 Sulphoacetaldehyde acetyltransferase

Contains

IPR000399 TPP-binding enzymes, conserved site

GO Term annotation Help

Function

GO:0003824 catalytic activity
GO:0030976 thiamin pyrophosphate binding

InterPro annotation

Entry Details in BioMart

Abstract

A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [1] that some of these enzymes are structurally related. This represents the C-terminal TPP binding domain of TPP enzymes.

Structural links Help

PDB - click here

SCOP: c.36.1.12 , c.36.1.9

CATH: 3.40.50.970

Database links Help

PANDIT: PF02775

Blocks: IPB011766

Pfam Clan: CL0254.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011766

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1L0T0 Acetolactate synthase-like protein

O61856 Acetolactate synthase-like protein

P06169 Pyruvate decarboxylase isozyme 1

P17597 Acetolactate synthase, chloroplastic

Q8BU33 Acetolactate synthase-like protein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012846	Acetolactate synthase, large subunit, biosynthetic
IPR012110	Pyruvate decarboxylase/indolepyruvate decarboxylase
IPR012001	Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
IPR012000	Thiamine pyrophosphate enzyme, central domain
IPR000399	TPP-binding enzymes, conserved site
IPR011766	Thiamine pyrophosphate enzyme, C-terminal TPP-binding
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Arjunan P, Umland T, Dyda F, Swaminathan S, Furey W, Sax M, Farrenkopf B, Gao Y, Zhang D, Jordan F. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. J. Mol. Biol. 256 590-600 1996 [PubMed: 8604141] http://dx.doi.org/10.1006/jmbi.1996.0111

Additional Reading Open in usermanual
	Berthold CL, Toyota CG, Moussatche P, Wood MD, Leeper F, Richards NG, Lindqvist Y. Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure 15 2007 853-61 [PubMed: 17637344] http://dx.doi.org/10.1016/j.str.2007.06.001
	Juan EC, Hoque MM, Hossain MT, Yamamoto T, Imamura S, Suzuki K, Sekiguchi T, Takenaka A. The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 900-7 [PubMed: 18007037]
	McCourt JA, Pang SS, King-Scott J, Guddat LW, Duggleby RG. Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase. Proc. Natl. Acad. Sci. U.S.A. 103 2006 569-73 [PubMed: 16407096] http://dx.doi.org/10.1073/pnas.0508701103
	Berthold CL, Gocke D, Wood MD, Leeper FJ, Pohl M, Schneider G. Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction. Acta Crystallogr. D Biol. Crystallogr. 63 2007 1217-24 [PubMed: 18084069] http://dx.doi.org/10.1107/S0907444907050433
	Bera AK, Polovnikova LS, Roestamadji J, Widlanski TS, Kenyon GL, McLeish MJ, Hasson MS. Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme. J. Am. Chem. Soc. 129 2007 4120-1 [PubMed: 17367138] http://dx.doi.org/10.1021/ja068636z

InterPro 23.1