Q3A246 (ARGJ_PELCD) 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:	Pcar_2322

Organism

Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]

Taxonomic identifier

338963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter

Protein attributes

Sequence length	393 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 – 178	178	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_0000227242
	Chain	179 – 393	215	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000227243
Sites
	Site	178 – 179	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3A246 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 8FBD89646345862D	FASTA	393	41,236
	10 20 30 40 50 60 MVKVNGFSFV ARSAGIRKSG KPDLGLIFST VPARCAGVFT TNKVQAAPVL VTAPRIAAGE 70 80 90 100 110 120 CQAVLVNSGN ANACTGEVGM QDALRCGQLA AKSLGIDEQL VAVSSTGVIG HPLPMPLLEK 130 140 150 160 170 180 TIPGMSEGLS ETAVDDVANA MMTTDSFAKV ASRQAGDSAP YTILGVAKGA GMIHPNMATM 190 200 210 220 230 240 LSFVMTDACV DQHFLQQALR QAVEGSFNII TVDRDTSTND MVLVLANGES KTPEIVADSA 250 260 270 280 290 300 EGQEFAELLR GVLLDLAKMI VRDGEGATKL VHVCVNGAAD DGDARKVAYN VATSNLVKTA 310 320 330 340 350 360 FFGEDANWGR IIAAVGYSEA QVDPSRIAIF FDGVPVVQKG LGTGPELEAQ ATDVLKQAEF 370 380 390 SVTIDLGLGD GRGEYYTSDL TYEYVKINAD YRT

References

[1]

"Complete sequence of Pelobacter carbinolicus DSM 2380." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000142 Genomic DNA. Translation: ABA89561.1.
RefSeq	YP_357731.1. NC_007498.2.
3D structure databases
ProteinModelPortal	Q3A246.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3A246.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3725014.
GenomeReviews	Gene locus Pcar_2322 in contig CP000142_GR.
KEGG	pca:Pcar_2322.
NMPDR	fig|338963.3.peg.698.
PATRIC	22890920. VBIPelCar86875_2510.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	GRDPNWG.
PhylomeDB	Q3A246.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	PCAR338963:PCAR_2322-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_PELCD

Accession

Primary (citable) accession number: Q3A246

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 22, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program