Reviewed, UniProtKB/Swiss-Prot Q07908 (ARGJ_BACST)

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

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
Enzyme regulation	Feedback inhibition by L-arginine.
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. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subunit structure	Heterotetramer of two alpha and two beta chains.
Subcellular location	CytoplasmProbable.
Miscellaneous	Independently synthesized alpha and beta subunits do not reconstitute a functional protein. Self-catalyzed precursor cleavage is a necessary step to form an active enzyme, probably by directing appropriate folding and/or topological organization of the active site. Some bacteria possess a monofunctional argJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
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	Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
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
Molecule processing
	Chain	1 – 196	196	Arginine biosynthesis bifunctional protein argJ alpha chain
	Chain	197 – 410	214	Arginine biosynthesis bifunctional protein argJ beta chain
Sites
	Site	196 – 197	2	Cleavage; by autolysis
Experimental info
	Mutagenesis	197	1	T → G: No autoproteolysis; loss of activity
	Mutagenesis	197	1	T → S or C: Low rate of intramolecular cleavage; loss of activity

Sequences

	Sequence		Length	Mass (Da)
	Q07908-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 00E948D64E8A8913	FASTA	410	43,377
	10 20 30 40 50 60 MTITKQTGQV TAVADGTVVT PEGFQAAGVN AGLRYSKNDL GVILCDVPAS AAAVYTQSHF 70 80 90 100 110 120 QAAPLKVTQA SLAVEQKLQA VIVNRPCANA CTGAQGLKDA YEMRELCAKQ FGLALHHVAV 130 140 150 160 170 180 ASTGVIGEYL PMEKIRAGIK QLVPGVTMAD AEAFQTAILT TDTVMKRACY QTTIDGKTVT 190 200 210 220 230 240 VGGAAKGSGM IHPNMATMLA FITTDANVSS PVLHAALRSI TDVSFNQITV DGDTSTNDMV 250 260 270 280 290 300 VVMASGLAGN DELTPDHPDW ENFYEALRKT CEDLAKQIAK DGEGATKLIE VRVRGAKTDE 310 320 330 340 350 360 EAKKIAKQIV GSNLVKTAVY GADANWGRII GAIGYSDAEV NPDNVDVAIG PMVMLKGSEP 370 380 390 400 410 QPFSEEEAAA YLQQETVVIE VDLHIGDGVG VAWGCDLTYD YVKINASYRT

References

[1]	"Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase." Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., Pierard P., Glansdorff N. J. Gen. Microbiol. 139:393-402(1993) [PubMed: 8473852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIB 8224 / CCM 2186.
[2]	"Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms." Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N., Sakanyan V. Eur. J. Biochem. 267:5217-5226(2000) [PubMed: 10931207] [Abstract] Cited for: CHARACTERIZATION. Strain: NCIB 8224 / CCM 2186.
[3]	"An invariant threonine is involved in self-catalyzed cleavage of the precursor protein for ornithine acetyltransferase." Marc F., Weigel P., Legrain C., Glansdorff N., Sakanyan V. J. Biol. Chem. 276:25404-25410(2001) [PubMed: 11320085] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF THR-197. Strain: NCIB 8224 / CCM 2186.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L06036 Genomic DNA. Translation: AAA22197.1.
PIR	I39766.
3D structure databases
SMR	Q07908. Positions 197-408.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
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.
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ARGJ_BACST

Accession

Primary (citable) accession number: Q07908

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	July 22, 2008
This is version 63 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)