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InterPro: IPR000796 Aspartate/other aminotransferase

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UniProtKB

Matches:

1707 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

IPR000796 Asp_trans

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00799	TRANSAMINASE	1492
PANTHER	PTHR11879	Asp_trans	1678
Signatures in BioMart

InterPro Relationships Help

Contains

IPR004838 Aminotransferases, class-I, pyridoxal-phosphate-binding site
IPR004839 Aminotransferase, class I/II
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1

GO Term annotation Help

Process

GO:0006520 cellular amino acid metabolic process

Function

GO:0008483 transaminase activity

InterPro annotation

Entry Details in BioMart

Abstract

Aspartate aminotransferase is important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. The enzyme catalyses the reaction:

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate-dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue [1]. This family includes some aromatic-amino-acid aminotransferases too.

Structural links Help

PDB - click here

SCOP: c.67.1.1

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

Enzyme: EC:2.6.1.1

Blocks: IPB000796

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000796

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P05201 Aspartate aminotransferase, cytoplasmic

P17174 Aspartate aminotransferase, cytoplasmic

P23542 Aspartate aminotransferase, cytoplasmic

P46248 Aspartate aminotransferase, chloroplastic

Q22067 Probable aspartate aminotransferase, cytoplasmic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site
IPR004839	Aminotransferase, class I/II
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
IPR000796	Aspartate/other aminotransferase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sung MH, Tanizawa K, Tanaka H, Kuramitsu S, Kagamiyama H, Hirotsu K, Okamoto A, Higuchi T, Soda K. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. J. Biol. Chem. 266 2567-72 1991 [PubMed: 1990006] http://intl.jbc.org/cgi/content/abstract/266/4/2567

Additional Reading Open in usermanual
	Islam MM, Goto M, Miyahara I, Ikushiro H, Hirotsu K, Hayashi H. Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step. Biochemistry 44 2005 8218-29 [PubMed: 15938611] http://dx.doi.org/10.1021/bi050071g
	Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D. Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms". Biochemistry 46 2007 10517-27 [PubMed: 17713924] http://dx.doi.org/10.1021/bi700663n
	Chow MA, McElroy KE, Corbett KD, Berger JM, Kirsch JF. Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase. Biochemistry 43 2004 12780-7 [PubMed: 15461450] http://dx.doi.org/10.1021/bi0487544
	Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H. Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. J. Biol. Chem. 278 2003 9481-8 [PubMed: 12488449] http://dx.doi.org/10.1074/jbc.M209235200
	Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H. Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Biochemistry 40 2001 353-60 [PubMed: 11148029] http://dx.doi.org/10.1021/bi001403e

InterPro 23.1