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:	GSU2049

From

Geobacter sulfurreducens

[TaxID: 35554]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; Geobacteraceae; Geobacter.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51573 / DSM 12127 / PCA;
DOI=10.1126/science.1088727; PubMed=14671304 [NCBI, ExPASy, EBI, Israel, Japan]
Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R., Fraser C.M.;
"Genome of Geobacter sulfurreducens: metal reduction in subsurface environments.";
Science 302:1967-1969(2003).

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

AE017180; AAR35425.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_953098.1; -.

3D structure databases

ModBase

P62061.

Protein family/group databases

MEROPS

T05.001; -.

Enzyme and pathway databases

BioCyc

GSUL243231:GSU_2049-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

P62061.

Genome annotation databases

GeneID

2686046; -.

GenomeReviews

AE017180_GR; GSU2049.

KEGG

gsu:GSU2049; -.

NMPDR

fig|243231.1.peg.2036; -.

TIGR

GSU2049; -.

Phylogenomic databases

HOGENOM

P62061; -.

Other

LinkHub

P62061; -.

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`	`1 178`	`178`	`Arginine biosynthesis bifunctional protein argJ alpha chain (By similarity).`	`PRO_0000002169`
`CHAIN`	`179 393`	`215`	`Arginine biosynthesis bifunctional protein argJ beta chain (By similarity).`	`PRO_0000002170`
`SITE`	`178 179`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 40986 Da [This is the MW of the unprocessed precursor]

CRC64: 8808BFB962CB9C57 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNVKGFRFSA VEAAIKKPGR LDLALICSDA PAAVAAVYTT NKVKAAPVLL DMERTTSGTC 

        70         80         90        100        110        120 
RAVVVNSGNA NACTGDRGME DARETTSLVA ERIGASEHEV LVCSTGVIGV PLPMERIRGG 

       130        140        150        160        170        180 
IPSLVAGLGS ATLDQIAAAI MTTDTFPKLE ARTGTAGGVG YTIAGIAKGA GMIMPNMATM 

       190        200        210        220        230        240 
LAFVVTDAAV DPQWLDRVFR RANDTSFNAI TVDGDMSTND TAIIMANGAA GNPVLSEGSE 

       250        260        270        280        290        300 
GAAEFAVLLE EVLLSLAKLI VKDGEGATKF VEVTVKGARS DADAKRAAMA VANSCLVKTA 

       310        320        330        340        350        360 
FFGQDANWGR IFAAVGYSGA DVEPDRAELF FDDVRMVQGG VFAGGDAEAR GTGVLRKKEF 

       370        380        390 
TVTVDLHLGD GRATVYTSDL SYDYVKINAD YRT

P62061 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