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:	BCE_4202

From

Bacillus cereus (strain ATCC 10987)

[TaxID: 222523]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh258; PubMed=14960714 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.";
Nucleic Acids Res. 32:977-988(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

AE017194; AAS43103.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_980495.1; -.

3D structure databases

ModBase

P62057.

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

P62057.

Genome annotation databases

GeneID

2747976; -.

GenomeReviews

AE017194_GR; BCE_4202.

KEGG

bca:BCE_4202; -.

NMPDR

fig|222523.1.peg.4167; -.

TIGR

BCE_4202; -.

Phylogenomic databases

HOGENOM

P62057; -.

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`	`1 193`	`193`	`Arginine biosynthesis bifunctional protein argJ alpha chain (By similarity).`	`PRO_0000002107`
`CHAIN`	`194 407`	`214`	`Arginine biosynthesis bifunctional protein argJ beta chain (By similarity).`	`PRO_0000002108`
`SITE`	`193 194`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 43899 Da [This is the MW of the unprocessed precursor]

CRC64: 0DD6BDAE57041021 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIKVASITKV ENGSIVTPKG FSAIGTAIGL KKEKKDLGAI VCDTPASCAA VYTTNQIQAA 

        70         80         90        100        110        120 
PLQVTKDSIA TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAEHFGL KENYVAVAST 

       130        140        150        160        170        180 
GVIGVPLPMD IIRNGIATLI PAKEEREAHS FSEAILTTDL ITKETCYEMV IDGEKVLIAG 

       190        200        210        220        230        240 
VAKGSGMIHP NMATMLSFIT TDAHIEHDVL QTTLSQITNH TFNQITIDGD TSTNDMVIVM 

       250        260        270        280        290        300 
ASGLSETKPI NMEHADWETF VFALQKVCED LAKKIAQDGE GATKLIEVNV LGARTNEEAK 

       310        320        330        340        350        360 
KIAKQIVGSS LVKTAIHGED PNWGRIISTI GQSEVAINPN TIDITLQSIA VLKNSEPQMF 

       370        380        390        400 
SEEEMKMRLQ EHEIMIDVNL HLGEETGSAW GCDLSYEYVK INACYRT

P62057 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