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 argJ1 alpha chain
Arginine biosynthesis bifunctional protein argJ1 beta chain

Gene name

	Name:	argJ1
	OrderedLocusNames:	alr2073

From

Anabaena sp. (strain PCC 7120)

[TaxID: 103690]

[HAMAP proteome]

Taxonomy

Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.;
"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.";
DNA Res. 8:205-213(2001).

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

BA000019; BAB73772.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AC2065; AC2065.

RefSeq

NP_486113.1; -.

3D structure databases

ModBase

Q8YVA8.

Protein family/group databases

MEROPS

T05.001; -.

Enzyme and pathway databases

BioCyc

NSP103690:ALR2073-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

Q8YVA8.

Genome annotation databases

GeneID

1105668; -.

GenomeReviews

BA000019_GR; alr2073.

KEGG

ana:alr2073; -.

NMPDR

fig|103690.1.peg.2380; -.

Phylogenomic databases

HOGENOM

Q8YVA8; -.

Genome annotation databases

CMR

Q8YVA8; alr2073.

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`	`1 190`	`190`	`Arginine biosynthesis bifunctional protein argJ1 alpha chain (By similarity).`	`PRO_0000002097`
`CHAIN`	`191 413`	`223`	`Arginine biosynthesis bifunctional protein argJ1 beta chain (By similarity).`	`PRO_0000002098`
`SITE`	`190 191`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 413 AA [This is the length of the unprocessed precursor]

Molecular weight: 42998 Da [This is the MW of the unprocessed precursor]

CRC64: 9268B3EA817D9134 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADWQEITGG ITAPKGYRAA GITAGLKPSG LPDLALIVSD VEAIASGVFT TSQVKAACVD 

        70         80         90        100        110        120 
YCRQRLQAKQ SARAILCNAG QANAATGSQG IKDAEESAEL LAKELNISPE LILLASTGVI 

       130        140        150        160        170        180 
GQRIKMDALR NGIPKLIASL TDTGSDAAAG AIITTDLVTK SIALETTIGD RPVRIGGIAK 

       190        200        210        220        230        240 
GSGMIHPNMA TMLAFVTCDA AVSSHLWQQM LTRAADRSFN SITVDGDTST NDSLIALANG 

       250        260        270        280        290        300 
QSRTPAITEV GAESEKLEAM LTAVCQHLAK AIARDGEGAT CLIEVQVTGA HDEQAARQIA 

       310        320        330        340        350        360 
KTIAGSSLVK SAIFGRDPNW GRIAAAAGRA GVPFEQENLQ IQLGDFLLLD NGQPLPFDRA 

       370        380        390        400        410 
AASAYLKQAA TGAYLQQDTV LISVKVGNGH GTGKAWGCDL SYDYVKINAE YTT

Q8YVA8 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