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:	MAP_1362

From

Mycobacterium paratuberculosis

[TaxID: 1770]

[HAMAP proteome]

Taxonomy

Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium avium complex (MAC).

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-968 / K-10;
DOI=10.1073/pnas.0505662102; PubMed=16116077 [NCBI, ExPASy, EBI, Israel, Japan]
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.;
"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).

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

AE016958; AAS03679.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_960296.1; -.

3D structure databases

ModBase

P62063.

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]

TIGRFAMs

TIGR00120; ArgJ; 1.

ProtoNet

P62063.

Genome annotation databases

GeneID

2719976; -.

GenomeReviews

AE016958_GR; MAP_1362.

KEGG

mpa:MAP1362; -.

NMPDR

fig|262316.1.peg.1362; -.

Phylogenomic databases

HOGENOM

P62063; -.

Genome annotation databases

CMR

P62063; MAP_1362.

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`	`1 199`	`199`	`Arginine biosynthesis bifunctional protein argJ alpha chain (By similarity).`	`PRO_0000002191`
`CHAIN`	`200 404`	`205`	`Arginine biosynthesis bifunctional protein argJ beta chain (By similarity).`	`PRO_0000002192`
`SITE`	`199 200`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 404 AA [This is the length of the unprocessed precursor]

Molecular weight: 40929 Da [This is the MW of the unprocessed precursor]

CRC64: C7F2E26D823E838C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTETVNAARL LREQGVTAPA GFRAAGIAAG IKASGKRDLA LVFNEGPDYG AAGVFTRNKV 

        70         80         90        100        110        120 
KAAPVLWSQQ VLTTGALRAV ILNSGGANAC TGPGGFQDAH ATAEAVAAAL SDWGTETGAI 

       130        140        150        160        170        180 
EVAVCSTGLI GDRLPMDKLL AGVRTIVQDM AGGLSGGDDA AQAIMTTDTV PKQVALHHPG 

       190        200        210        220        230        240 
NWTVGGMAKG AGMIAPSLAT MLCVLTTDAA VDPVALDTAL RRATAATFDR LDIDGACSTN 

       250        260        270        280        290        300 
DTVLLLASGA SGITPAQADL DDAVLRVCDD LCAQLQADAE GVTKRVNVTV TGAASDDDAV 

       310        320        330        340        350        360 
VAARTIARDS LVKTAVFGSD PNWGRVVAAV GIAPIALDPD RMTVSFNGSA VFADGVGTPG 

       370        380        390        400 
AREVDLSGPD IDITVDLRLG DGRATVRTTD LSHGYVEENS AYSS

P62063 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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