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:	PMT2135

From

Prochlorococcus marinus (strain MIT 9313)

[TaxID: 74547]

[HAMAP proteome]

Taxonomy

Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(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

BX572101; CAE22309.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_895959.1; -.

3D structure databases

ModBase

Q7V436.

Protein family/group databases

MEROPS

T05.001; -.

Enzyme and pathway databases

BioCyc

PMAR74547:PMT2135-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

Q7V436.

Genome annotation databases

GeneID

1727636; -.

GenomeReviews

BX548175_GR; PMT2135.

KEGG

pmt:PMT2135; -.

NMPDR

fig|74547.1.peg.2126; -.

Phylogenomic databases

HOGENOM

Q7V436; -.

Genome annotation databases

CMR

Q7V436; PMT2135.

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`	`1 210`	`210`	`Arginine biosynthesis bifunctional protein argJ alpha chain (By similarity).`	`PRO_0000002209`
`CHAIN`	`211 427`	`217`	`Arginine biosynthesis bifunctional protein argJ beta chain (By similarity).`	`PRO_0000002210`
`SITE`	`210 211`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 44318 Da [This is the MW of the unprocessed precursor]

CRC64: AAC9BCFA7C311F12 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALVEDVFSL SPKAVSSALA SLWRPIQGGV SAPLGFQAAG ITAGLKDSGK PDLALLLAPE 

        70         80         90        100        110        120 
GAVCAGMFTT SLVRAACVDL CVDHLQACGG KARAVLINSG QANACTGERG WLDSLRASQA 

       130        140        150        160        170        180 
LAGRLELPVE QVLICSTGVI GVPIPMDTLL AGLDPLVEAL SDEGGAEAAG AILTTDLVEK 

       190        200        210        220        230        240 
QFALEAELGG RSVRIGGMAK GSGMIHPDMA TMLGYLSCDV GVEVDAWQAM LKRVVDCSFN 

       250        260        270        280        290        300 
AMTVDGDTST NDSCLAFAAG ELLEQEHLQA LEAGLLVAAQ QLAKAIARDG EGATCLLEVQ 

       310        320        330        340        350        360 
VEGVVGDVEA RRIARTVCGS SLVKTAVHGR DPNWGRIVAA AGCAGVPFDP AAVALWLGPH 

       370        380        390        400        410        420 
QLMEFGEPLP FDRLAASRYM QERVDGSYLC DDTVQIRLVV GDGSGDGMAW GCDLSDQYVR 


INADYTT

Q7V436 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