Glutamate N-acetyltransferase
     (EC 2.3.1.35)
     (Ornithine acetyltransferase)
     (OATase)
     (Ornithine transacetylase)
Amino-acid acetyltransferase
     (EC 2.3.1.1)
     (N-acetylglutamate synthase)
     (AGS)

Contains

Arginine biosynthesis bifunctional protein argJ alpha chain
Arginine biosynthesis bifunctional protein argJ beta chain

Gene name

Name:

argJ

From

Bacillus stearothermophilus (Geobacillus stearothermophilus)

[TaxID: 1422]

Taxonomy

Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NCIB 8224 / CCM 2186; PubMed=8473852 [NCBI, ExPASy, EBI, Israel, Japan] Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., Pierard P., 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).
[2]	CHARACTERIZATION. STRAIN=NCIB 8224 / CCM 2186; PubMed=10931207 [NCBI, ExPASy, EBI, Israel, Japan] Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N., Sakanyan V.; "Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms."; Eur. J. Biochem. 267:5217-5226(2000).
[3]	CHARACTERIZATION, AND MUTAGENESIS OF THR-197. STRAIN=NCIB 8224 / CCM 2186; DOI=10.1074/jbc.M100392200; PubMed=11320085 [NCBI, ExPASy, EBI, Israel, Japan] Marc F., Weigel P., Legrain C., Glansdorff N., Sakanyan V.; "An invariant threonine is involved in self-catalyzed cleavage of the precursor protein for ornithine acetyltransferase."; J. Biol. Chem. 276:25404-25410(2001).

Comments

FUNCTION: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
CATALYTIC ACTIVITY: N²-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate.
CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
ENZYME REGULATION: Feedback inhibition by L-arginine.
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1 .
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4 .
SUBUNIT: Heterotetramer of two alpha and two beta chains.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
MISCELLANEOUS: Independently synthesized alpha and beta subunits do not reconstitute a functional protein. Self-catalyzed precursor cleavage is a necessary step to form an active enzyme, probably by directing appropriate folding and/or topological organization of the active site.
MISCELLANEOUS: Some bacteria possess a monofunctional argJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
SIMILARITY: Belongs to the argJ family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L06036; AAA22197.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I39766; I39766.

3D structure databases

SMR

Q07908; 197-408.

ModBase

Q07908.

Protein family/group databases

MEROPS

T05.001; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004042;	Molecular function: amino-acid N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0004358;	Molecular function: glutamate N-acetyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01106; -; 1.
PBIL [Tree]

InterPro

IPR002813; Arg_biosynth_ArgJ.
Graphical view of domain structure.

PANTHER

PTHR23100; ArgJ; 1.

Pfam

PF01960; ArgJ; 1.
Pfam graphical view of domain structure.

ProDom

PD004193; ArgJ; 2.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR00120; ArgJ; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Multifunctional enzyme; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 196`	`196`	`Arginine biosynthesis bifunctional protein argJ alpha chain.`	`PRO_0000002119`
`CHAIN`	`197 410`	`214`	`Arginine biosynthesis bifunctional protein argJ beta chain.`	`PRO_0000002120`
`SITE`	`196 197`	`2`	`Cleavage; by autolysis.`
`MUTAGEN`	`197 197`		`T->G: No autoproteolysis; loss of activity.`
`MUTAGEN`	`197 197`		`T->S,C: Low rate of intramolecular cleavage; loss of activity.`

Sequence information

Length: 410 AA [This is the length of the unprocessed precursor]

Molecular weight: 43377 Da [This is the MW of the unprocessed precursor]

CRC64: 00E948D64E8A8913 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTITKQTGQV TAVADGTVVT PEGFQAAGVN AGLRYSKNDL GVILCDVPAS AAAVYTQSHF 

        70         80         90        100        110        120 
QAAPLKVTQA SLAVEQKLQA VIVNRPCANA CTGAQGLKDA YEMRELCAKQ FGLALHHVAV 

       130        140        150        160        170        180 
ASTGVIGEYL PMEKIRAGIK QLVPGVTMAD AEAFQTAILT TDTVMKRACY QTTIDGKTVT 

       190        200        210        220        230        240 
VGGAAKGSGM IHPNMATMLA FITTDANVSS PVLHAALRSI TDVSFNQITV DGDTSTNDMV 

       250        260        270        280        290        300 
VVMASGLAGN DELTPDHPDW ENFYEALRKT CEDLAKQIAK DGEGATKLIE VRVRGAKTDE 

       310        320        330        340        350        360 
EAKKIAKQIV GSNLVKTAVY GADANWGRII GAIGYSDAEV NPDNVDVAIG PMVMLKGSEP 

       370        380        390        400        410 
QPFSEEEAAA YLQQETVVIE VDLHIGDGVG VAWGCDLTYD YVKINASYRT

Q07908 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools