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
	OrderedLocusNames:	GK0791

From

Geobacillus kaustophilus

[TaxID: 1462]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HTA426;
DOI=10.1093/nar/gkh970; PubMed=15576355 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.;
"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus.";
Nucleic Acids Res. 32:6292-6303(2004).

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 (By similarity).
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.
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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Probable).
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

BA000043; BAD75076.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_146644.1; -.

3D structure databases

SMR

Q5L1V4; 197-408.

ModBase

Q5L1V4.

Protein family/group databases

MEROPS

T05.001; -.

Enzyme and pathway databases

BioCyc

GKAU235909:GK0791-MON; -.

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]

TIGRFAMs

TIGR00120; ArgJ; 1.

ProtoNet

Q5L1V4.

Genome annotation databases

3185135; -.

BA000043_GR; GK0791.

gka:GK0791; -.

fig|235909.3.peg.1442; -.

Phylogenomic databases

HOGENOM

Q5L1V4; -.

Genome annotation databases

CMR

Q5L1V4; GK0791.

Other

UniRef

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

Keywords

Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; 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 (By similarity).`	`PRO_0000227228`
`CHAIN`	`197 410`	`214`	`Arginine biosynthesis bifunctional protein argJ beta chain (By similarity).`	`PRO_0000227229`
`SITE`	`196 197`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

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

Molecular weight: 43476 Da [This is the MW of the unprocessed precursor]

CRC64: DF461D99F0376E69 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTATKQTAQV TAVADGTVVT PKGFQAAGVH AGLRYSKKDL GVILCDVPAS AAAVYTQSHF 

        70         80         90        100        110        120 
QAAPLKVTQA SLAVEQKLQA VIVNSACANA CTGEQGLKDA YEMRELCAKQ FGLALHHVAV 

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

       190        200        210        220        230        240 
VGGAAKGSGM IHPNMATMLA FITTDANISS AVLHDALRSI TDVSFNQITV DGDTSTNDMV 

       250        260        270        280        290        300 
VVMASGLAGN DELTPNHPDW EHFYEALRKT CEDLAKQIAR DGEGATKLIE VRVRGAKTDE 

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

       370        380        390        400        410 
QPFSEEEATA YLQQETVVIE VDLHLGDGFG VAWGCDLTYD YVKINASYRT

Q5L1V4 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