Reviewed, UniProtKB/Swiss-Prot Q818W0 (ARGJ_BACCR)

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:	BC_4129

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

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

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. 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 – 194	194	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002109
	Chain	195 – 408	214	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002110
Sites
	Site	194 – 195	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q818W0-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: CAE87F7994699E22	FASTA	408	43,961
	10 20 30 40 50 60 MMIKVASITK LENGSIVTPK GFSAIGTVNG LKKEKKDLGA IVCDVPASCA AVYTTNQIQA 70 80 90 100 110 120 APLQVTKDSI TAEGKLQAII VNSGNANACT GMQGLQDAYE MRVLGAEHFG MKENYVAVAS 130 140 150 160 170 180 TGVIGVPLPM DIIRKGVATL IPTKEESEAY SFSEAILTTD LITKETCYEM IIDGKKVVIA 190 200 210 220 230 240 GVAKGSGMIH PNMATMLSFI TTDAHIEHNV LQTALSQITN HTFNQITVDG DTSTNDMVIV 250 260 270 280 290 300 MASGLSETRP INMEHTDWET FVGALQKVCE DLAKKIAQDG EGATKLIEVN VLGAQTNEEA 310 320 330 340 350 360 KKIAKQIVGS SLVKTAIHGE DPNWGRIISS IGQSEVAINP NTIDITLQSI SVLKNSEPQT 370 380 390 400 FSEEKMKERL QEDEIVINVY LHLGEETGSA WGCDLSYEYV KINACYRT

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP11047.1.
RefSeq	NP_833846.1.
3D structure databases
SMR	Q818W0. Positions 4-194, 18-404, 195-406.
ModBase	Search...
Protein-protein interaction databases
STRING	Q818W0.
Genome annotation databases
GeneID	1206474.
GenomeReviews	Gene locus BC_4129 in contig AE016877_GR.
KEGG	bce:BC4129.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	QNRFCAA.
Enzyme and pathway databases
BioCyc	BCER226900:BC_4129-MONOMER.
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_BACCR

Accession

Primary (citable) accession number: Q818W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 49 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)