Q57AV8 (ARGJ_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ

Cleaved into the following 2 chains:

1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
2. Arginine biosynthesis bifunctional protein ArgJ beta chain

Including the following 2 domains:

1. Glutamate N-acetyltransferase
   EC=2.3.1.35
   Alternative name(s):
   Ornithine acetyltransferase
   Short name=OATase
   Ornithine transacetylase
2. Amino-acid acetyltransferase
   EC=2.3.1.1
   Alternative name(s):
   N-acetylglutamate synthase
   Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	BruAb1_1917

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	413 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.
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
PTM	Autocatalytic cleavage
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 194	194	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_0000227208
	Chain	195 – 413	219	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000227209
Sites
	Site	194 – 195	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57AV8 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 44C1DEF0E4A63B04	FASTA	413	43,244
	10 20 30 40 50 60 MSASVSPLAP KHYPAMPVIH GVRIATAAAG IKYKGRTDLM LMVFDRPAEA AGVFTRSLCP 70 80 90 100 110 120 SAPVDFCRRN LVHGKARAVV VNSGNANAFT GLKGREATQA TAEAAAKAIG CATTDIFLAS 130 140 150 160 170 180 TGVIGEPLDA GKFSHLLGDM AESATEDFWT EAAKAIMTTD TYPKVATETV LLGQVPVTIN 190 200 210 220 230 240 GIAKGAGMIA PDMATMLSFV VTDAPIKADA LQSLLSKGVG STFNSVTVDS DTSTSDTLML 250 260 270 280 290 300 FATGTAAERG APEITDAADK RLADFKKALG RVLKSLALQV VRDGEGARKM VEVEVTGAKS 310 320 330 340 350 360 AASAKKIALS IANSPLVKTA VAGEDANWGR VVMAVGKAGE PADRDRLAIW FGDIRVAHQG 370 380 390 400 410 ERDPAYSEDA TSAYMEGEDI RIRVDLGIGR GKATVWTCDL TKEYVAINGD YRS

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX75226.1.
RefSeq	YP_222587.1. NC_006932.1.
3D structure databases
ProteinModelPortal	Q57AV8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3340537.
GenomeReviews	Gene locus BruAb1_1917 in contig AE017223_GR.
KEGG	bmb:BruAb1_1917.
PATRIC	17825663. VBIBruAbo15061_2024.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284202.
OMA	FPKLATR.
PhylomeDB	Q57AV8.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	BABO262698:BRUAB1_1917-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
KO	K00620.
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_BRUAB

Accession

Primary (citable) accession number: Q57AV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 10, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program