Q5WEW8 (ARGJ_BACSK) 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:	ABC2557

Organism

Bacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]

Taxonomic identifier

66692 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	408 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_0000002117
	Chain	195 – 408	214	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000002118
Sites
	Site	194 – 195	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5WEW8 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 45C55C81659F1AEB	FASTA	408	42,826
	10 20 30 40 50 60 MLTKQTTGQA WKQIKGSITD VKGFTTAGAH CGLKRKRLDI GAIFCDVPAN AAGVFTLNQI 70 80 90 100 110 120 QAAPLKVTKE SLAHSNGKLQ AVLVNSGNAN ACTGASGLVD AYEMRALAAA KFAVPEEMVA 130 140 150 160 170 180 VTSTGVIGEK MPMEKVRSGI EDLVLSKEST PFAEAILTTD TGTKEVCVEV VIDQKTVRIA 190 200 210 220 230 240 GVAKGSGMIH PNMATMLGFI TTDANIETAA LKRALAKATD ETFNRITVDG DTSTNDMVLV 250 260 270 280 290 300 LASGLADNQP LDETHPDWAN FYGALSACAE SLAKKIAKDG EGATKLIEVQ VAGAVSDEEA 310 320 330 340 350 360 GKVAKAIVGS DLVKTAAYGK DGNWGRIICA IGYSGCTLDP DTIDIAIGPY ETLVQSEPVV 370 380 390 400 VDDAAISKYM EAETIVIKAD LHQGQGVGKA WGCDLTYDYV RINAGYRT

References

[1]

"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16." Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KSM-K16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006627 Genomic DNA. Translation: BAD65092.1.
RefSeq	YP_176053.1. NC_006582.1.
3D structure databases
ProteinModelPortal	Q5WEW8.
SMR	Q5WEW8. Positions 7-406.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5WEW8.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000047728; EBBACP00000046489; EBBACG00000047719.
GeneID	3201719.
GenomeReviews	Gene locus ABC2557 in contig AP006627_GR.
KEGG	bcl:ABC2557.
NMPDR	fig|66692.3.peg.2245.
PATRIC	18924756. VBIBacCla58185_2730.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
GeneTree	EBGT00050000002382.
HOGENOM	HBG284202.
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	BCLA66692:ABC2557-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_BACSK

Accession

Primary (citable) accession number: Q5WEW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program