Reviewed, UniProtKB/Swiss-Prot Q3JNE9 (ARGJ_BURP1)

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:	BURPS1710b_3534

Organism

Burkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]

Taxonomic identifier

320372 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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. 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 – 196	196	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000227210
	Chain	197 – 413	217	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000227211
Sites
	Site	196 – 197	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3JNE9-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 990513FF806E3EE1	FASTA	413	43,061
	10 20 30 40 50 60 MAVNFPSIDP AQLHPVAGVT LGWAEANIRK PNRKDVLVVS VEEGATVSGV FTENRFCAAP 70 80 90 100 110 120 VTVCREHLAK VRAGGAGIRA LVVNTGNANA GTGEPGLAHA RETCAELARL AGIAPGQVLP 130 140 150 160 170 180 FSTGVILEPL PIERLKAGLP AALANRAAAN WHDAAQAIMT TDTLPKAASR QVTIDGHTIT 190 200 210 220 230 240 LTGISKGAGM IKPNMATMLG FLAFDAKVAQ PVLDALVKDV ADRSFNCITI DGDTSTNDSF 250 260 270 280 290 300 ILIASGKASL PQIASTDSPA YAALREAVTA VAQALAQLIV RDGEGATKFI TVTVEGGKSA 310 320 330 340 350 360 AECRQIAYAI GHSPLVKTAF YASDPNLGRI LAAIGYAGVA DLDVGKIDLY LDDVLVAKAG 370 380 390 400 410 GRNPAYLEED GQRVMKQSEI AVRVLLGRGD AQATIWTCDL SHDYVSINAD YRS

References

[1]	Woods D.E., Nierman W.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000124 Genomic DNA. Translation: ABA49184.1.
RefSeq	YP_334904.1.
3D structure databases
SMR	Q3JNE9. Positions 7-196, 17-410, 197-411.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3JNE9.
Genome annotation databases
GeneID	3690529.
GenomeReviews	Gene locus BURPS1710b_3534 in contig CP000124_GR.
KEGG	bpm:BURPS1710b_3534.
TIGR	BURPS1710b_3534.
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	QNRFCAA.
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_BURP1

Accession

Primary (citable) accession number: Q3JNE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 8, 2005
Last modified:	February 9, 2010
This is version 33 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)