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InterPro: IPR004839 Aminotransferase, class I/II

Protein matches Help

UniProtKB

Matches:

21903 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

IPR004839 Aminotransferase_I/II

Secondary

IPR001511

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00155	Aminotran_1_2	21903
Signatures in BioMart

InterPro Relationships Help

Parent

IPR015424 Pyridoxal phosphate-dependent transferase, major domain

Children

IPR005958 Tyrosine/nicotianamine aminotransferase
IPR010961 Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase
IPR019877 Succinyldiaminopimelate transaminase
IPR019878 Succinyldiaminopimelate transaminase, beta/gammaproteobacteria
IPR019880 Succinyldiaminopimelate transaminase, actinobacteria
IPR019881 LL-diaminopimelate aminotransferase

Found in

IPR000796 Aspartate/other aminotransferase
IPR001176 1-aminocyclopropane-1-carboxylate synthase
IPR004723 8-amino-7-oxononanoate synthase
IPR005860 L-threonine-O-3-phosphate decarboxylase
IPR005861 Histidinol-phosphate aminotransferase
IPR010962 Pyridoxal phosphate-dependent acyltransferase, putative
IPR011282 2-amino-3-ketobutyrate coenzyme A ligase
IPR019942 LL-diaminopimelate aminotransferase, plant-related

Contains

IPR001917 Aminotransferase, class-II, pyridoxal-phosphate binding site
IPR004838 Aminotransferases, class-I, pyridoxal-phosphate-binding site
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016769 transferase activity, transferring nitrogenous groups
GO:0030170 pyridoxal phosphate binding

InterPro annotation

Entry Details in BioMart

Abstract

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. On the basis of sequence similarity, these various enzymes can be grouped [1] into class I and class II. This entry includes proteins from both subfamilies.

Structural links Help

PDB - click here

SCOP: c.67.1.1 , c.67.1.3 , c.67.1.4

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

Enzyme: EC:2

PANDIT: PF00155

Blocks: IPB004839

Pfam Clan: CL0061.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004839

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P08680 5-aminolevulinate synthase, erythroid-specific, mitochondrial

P17174 Aspartate aminotransferase, cytoplasmic

P23542 Aspartate aminotransferase, cytoplasmic

Q22067 Probable aspartate aminotransferase, cytoplasmic

Q93ZN9 LL-diaminopimelate aminotransferase, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019942	LL-diaminopimelate aminotransferase, plant-related
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
IPR010961	Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR001917	Aminotransferase, class-II, pyridoxal-phosphate binding site
IPR000796	Aspartate/other aminotransferase
IPR015118	5-aminolevulinate synthase presequence
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	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
	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
	Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG. Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine. FEBS Lett. 579 2005 2458-62 [PubMed: 15848188] http://dx.doi.org/10.1016/j.febslet.2005.03.048
	Alexeev D, Baxter RL, Campopiano DJ, Kerbarh O, Sawyer L, Tomczyk N, Watt R, Webster SP. Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine. Org. Biomol. Chem. 4 2006 1209-12 [PubMed: 16557306] http://dx.doi.org/10.1039/b517922j
	Han Q, Gao YG, Robinson H, Li J. Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase. Biochemistry 47 2008 1622-30 [PubMed: 18186649] http://dx.doi.org/10.1021/bi701800j
	Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. Biochemistry 38 1999 2413-24 [PubMed: 10029535] http://dx.doi.org/10.1021/bi9819881
	Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Acta Crystallogr. D Biol. Crystallogr. 55 1999 1474-7 [PubMed: 10417420] http://dx.doi.org/10.1107/S0907444999006630
	Han Q, Gao YG, Robinson H, Ding H, Wilson S, Li J. Crystal structures of Aedes aegypti kynurenine aminotransferase. FEBS J. 272 2005 2198-206 [PubMed: 15853804] http://dx.doi.org/10.1111/j.1742-4658.2005.04643.x

InterPro 23.1