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InterPro: IPR004450 Threonine synthase

Protein matches Help

UniProtKB

Matches:

1833 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

IPR004450 Thr_synthase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00260	thrC	1833
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001926 Pyridoxal phosphate-dependent enzyme, beta subunit

Contains

IPR000634 Serine/threonine dehydratase, pyridoxal-phosphate-binding site

GO Term annotation Help

Process

GO:0009088 threonine biosynthetic process

Function

GO:0004795 threonine synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

Threonine synthase (EC: 4.2.3.1) is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate, using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes [1].

Structural links Help

PDB - click here

SCOP: c.79.1.1

CATH: 3.40.50.1100 , 3.90.1380.10

Database links Help

Enzyme: EC:4.2.3.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004450

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P16120 Threonine synthase

P74193 Threonine synthase

Q80W22 Threonine synthase-like 2

Q8IYQ7 Threonine synthase-like 1

Q9S7B5 Threonine synthase 1, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000634	Serine/threonine dehydratase, pyridoxal-phosphate-binding site
IPR004450	Threonine synthase
IPR000623	Shikimate kinase
IPR001926	Pyridoxal phosphate-dependent enzyme, beta subunit
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Parsot C. Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. EMBO J. 5 3013-9 1986 [PubMed: 3098560] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3098560

Additional Reading Open in usermanual
	Omi R, Goto M, Miyahara I, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K. Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism. J. Biol. Chem. 278 2003 46035-45 [PubMed: 12952961] http://dx.doi.org/10.1074/jbc.M308065200
	Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. J. Biol. Chem. 277 2002 12396-405 [PubMed: 11756443] http://dx.doi.org/10.1074/jbc.M108734200
	Thomazeau K, Curien G, Dumas R, Biou V. Crystal structure of threonine synthase from Arabidopsis thaliana. Protein Sci. 10 2001 638-48 [PubMed: 11344332] http://dx.doi.org/10.1110/ps.44301

InterPro 23.1