Reviewed, UniProtKB/Swiss-Prot Q6FED8 (ARGJ_ACIAD)

Names and origin

Protein names

Recommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	ACIAD0650

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_01106
Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106
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. HAMAP MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106
Subunit structure	Heterotetramer of two alpha and two beta chains By similarity. HAMAP MF_01106
Subcellular location	Cytoplasm Probable HAMAP MF_01106.
Miscellaneous	Some bacteria possess a monofunctional argJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106
Sequence similarities	Belongs to the argJ family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 189	189	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002093
	Chain	190 – 406	217	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002094
Sites
	Site	189 – 190	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FED8-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 55FEE68AD5206727	FASTA	406	43,579
	10 20 30 40 50 60 MAVGDVTMPH MHVVNGVKIG STEAYVRYPN RRDLVVFKFV EGSHVAGVFT QSAFAAAPVL 70 80 90 100 110 120 VSKKHLAESA IRYLIINTGN ANAATGQTGV INAQKTCTKL AELAGVESSQ VLPFSTGVIG 130 140 150 160 170 180 EQLPIERLLD GIQPALQDLK DDAWTEAAFG IMTTDTTPKG ASEQFELDGV VYTMTGISKG 190 200 210 220 230 240 AGMIRPNMAT MLSFVATDAP ISQSLVQTLL KTTVEQSFNR ITIDGDTSTN DSCIFVATGQ 250 260 270 280 290 300 AGGVEISSEQ DPRYSKILEI LQRIMNRLAQ LIVRDGEGAT KFITVAVEGG ENTQECCDVA 310 320 330 340 350 360 YSIAHSPLIK TAVFASDPNW GRIVMAIGKA GVPQLDVSKV QVWLDDVQIC RDGGAAADYT 370 380 390 400 EEQGARVMAQ AEMTIRVDLG RGTAKDTVYT CDLSYDYVKI NADYRS

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67570.1.
RefSeq	YP_045392.1.
3D structure databases
SMR	Q6FED8. Positions 15-403, 190-404.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FED8.
Genome annotation databases
GeneID	2877981.
GenomeReviews	Gene locus ACIAD0650 in contig CR543861_GR.
KEGG	aci:ACIAD0650.
NMPDR	fig|62977.3.peg.295.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	QNRFCAA.
PhylomeDB	Q6FED8.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0650-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_ACIAD

Accession

Primary (citable) accession number: Q6FED8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)