Reviewed, UniProtKB/Swiss-Prot P62057 (ARGJ_BACC1)

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:	BCE_4202

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	407 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.
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.
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	amino-acid 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 – 193	193	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002107
	Chain	194 – 407	214	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002108
Sites
	Site	193 – 194	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62057-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 0DD6BDAE57041021	FASTA	407	43,899
	10 20 30 40 50 60 MIKVASITKV ENGSIVTPKG FSAIGTAIGL KKEKKDLGAI VCDTPASCAA VYTTNQIQAA 70 80 90 100 110 120 PLQVTKDSIA TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAEHFGL KENYVAVAST 130 140 150 160 170 180 GVIGVPLPMD IIRNGIATLI PAKEEREAHS FSEAILTTDL ITKETCYEMV IDGEKVLIAG 190 200 210 220 230 240 VAKGSGMIHP NMATMLSFIT TDAHIEHDVL QTTLSQITNH TFNQITIDGD TSTNDMVIVM 250 260 270 280 290 300 ASGLSETKPI NMEHADWETF VFALQKVCED LAKKIAQDGE GATKLIEVNV LGARTNEEAK 310 320 330 340 350 360 KIAKQIVGSS LVKTAIHGED PNWGRIISTI GQSEVAINPN TIDITLQSIA VLKNSEPQMF 370 380 390 400 SEEEMKMRLQ EHEIMIDVNL HLGEETGSAW GCDLSYEYVK INACYRT

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS43103.1.
RefSeq	NP_980495.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	2747976.
GenomeReviews	Gene locus BCE_4202 in contig AE017194_GR.
KEGG	bca:BCE_4202.
NMPDR	fig|222523.1.peg.4167.
TIGR	BCE_4202.
Phylogenomic databases
HOGENOM	P62057.
OMA	P62057. IVNSGNA.
Family and domain databases
HAMAP	MF_01106. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. ArgJ. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_BACC1

Accession

Primary (citable) accession number: P62057

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	June 16, 2009
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)