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InterPro: IPR002813 Arginine biosynthesis protein ArgJ

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1104 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
Matches in BioMart

Accession

IPR002813 Arg_biosynth_ArgJ

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_01106	Arg_biosynth_ArgJ	857
Pfam	PF01960	ArgJ	1104
PANTHER	PTHR23100	ArgJ	1094
TIGRFAMs	TIGR00120	ArgJ	1070
Signatures in BioMart

InterPro Relationships Help

Contains

IPR016117 Peptidase S58 DmpA/arginine biosynthesis protein ArgJ

GO Term annotation Help

Process

GO:0006526 arginine biosynthetic process

Function

GO:0004358 glutamate N-acetyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

ArgJ is a bifunctional protein that catalyses the first EC:2.3.1.35 and fifth steps EC:2.3.1.1 in arginine biosynthesis [1]. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase; EC:2.3.1.35), an ArgJ-like protein from Streptomyces clavuligerus [2].

Structural links Help

PDB - click here

SCOP: d.154.1.2

Database links Help

Enzyme: EC:2.3.1.1 , EC:2.3.1.35

PANDIT: PF01960

Blocks: IPB002813

CluSTr: ALLvsALL:37590:74

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002813

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A4FXT1 Arginine biosynthesis bifunctional protein argJ

O94346 Probable arginine biosynthesis bifunctional protein arg7, mitochondrial

P74122 Arginine biosynthesis bifunctional protein argJ

Q04728 Arginine biosynthesis bifunctional protein ARG7, mitochondrial

Q53940 Glutamate N-acetyltransferase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002813	Arginine biosynthesis protein ArgJ
IPR016117	Peptidase S58 DmpA/arginine biosynthesis protein ArgJ
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Sakanyan V, Charlier D, Legrain C, Kochikyan A, Mett I, Pierard A, Glansdorff N. Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase. J. Gen. Microbiol. 139 393-402 1993 [PubMed: 8473852]
2.	Elkins JM, Kershaw NJ, Schofield CJ. X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem. J. 385 565-73 2005 [PubMed: 15352873] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=15352873&action=stream&blobtype=pdf

InterPro 23.1