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InterPro: IPR001597 Aromatic amino acid beta-eliminating lyase/threonine aldolase

Protein matches Help

UniProtKB

Matches:

1750 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

IPR001597 ArAA_b-elim_lyase/Thr_aldolase

Secondary

IPR011166

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01212	Beta_elim_lyase	1750
Signatures in BioMart

InterPro Relationships Help

Found in

IPR011166 Tryptophanase
IPR013440 Tryptophanase, proteobacteria
IPR013441 Tyrosine phenol-lyase
IPR015424 Pyridoxal phosphate-dependent transferase, major domain

Contains

IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR018176 Tryptophanase, conserved site

GO Term annotation Help

Process

GO:0006520 cellular amino acid metabolic process

Function

GO:0016829 lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in many tryptophanases (tryptophan indole-lyase, TNase), tyrosine phenol-lyases (TPL) and threonine aldolases. It is involved in the degradation of amino acids. The glycine cleavage system is composed of four proteins: P, T, L and H. In Bacillus subtilis, the P 'protein' is an heterodimer of two subunits. The glycine cleavage system catalyses the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein

Structural links Help

PDB - click here

SCOP: c.67.1.1 , c.67.1.2

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

PANDIT: PF01212

Blocks: IPB001597

COMe: PRX000853

Pfam Clan: CL0061.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001597

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B0R7Q6 Probable tryptophanase

O13427 Threonine aldolase

P0A853 Tryptophanase

P37303 Low specificity L-threonine aldolase

Q21890 Uncharacterized protein R102.4

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015424	Pyridoxal phosphate-dependent transferase, major domain
IPR015422	Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR001597	Aromatic amino acid beta-eliminating lyase/threonine aldolase
IPR018176	Tryptophanase, conserved site
IPR013440	Tryptophanase, proteobacteria
IPR011166	Tryptophanase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Ku SY, Yip P, Howell PL. Structure of Escherichia coli tryptophanase. Acta Crystallogr. D Biol. Crystallogr. 62 2006 814-23 [PubMed: 16790938] http://dx.doi.org/10.1107/S0907444906019895
	Kielkopf CL, Burley SK. X-ray structures of threonine aldolase complexes: structural basis of substrate recognition. Biochemistry 41 2002 11711-20 [PubMed: 12269813] http://dx.doi.org/10.1021/bi020393+
	Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O. The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation. Acta Crystallogr. D Biol. Crystallogr. 63 2007 969-74 [PubMed: 17704565] http://dx.doi.org/10.1107/S0907444907036396
	Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH. Crystal structure of tryptophanase. J. Mol. Biol. 276 1998 603-23 [PubMed: 9551100] http://dx.doi.org/10.1006/jmbi.1997.1561
	Milic D, Matkovic-Calogovic D, Demidkina TV, Kulikova VV, Sinitzina NI, Antson AA. Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions. Biochemistry 45 2006 7544-52 [PubMed: 16768450] http://dx.doi.org/10.1021/bi0601858

InterPro 23.1