Q07908 (ARGJ_GEOSE) 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

Organism

Geobacillus stearothermophilus (Bacillus 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 further processed into a mature form.
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. 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
Enzyme regulation	Feedback inhibition by L-arginine. 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.
Subcellular location	Cytoplasm Probable HAMAP MF_01106.
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. HAMAP MF_01106 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	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 – 196	196	Arginine biosynthesis bifunctional protein ArgJ alpha chain HAMAP MF_01106		PRO_0000002119
	Chain	197 – 410	214	Arginine biosynthesis bifunctional protein ArgJ beta chain HAMAP MF_01106		PRO_0000002120
Sites
	Site	196 – 197	2	Cleavage; by autolysis
Experimental info
	Mutagenesis	197	1	T → G: No autoproteolysis; loss of activity. Ref.3
	Mutagenesis	197	1	T → S or C: Low rate of intramolecular cleavage; loss of activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q07908 [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: NCIMB 8224 / CCM 2186 / VKM B-718.
[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: NCIMB 8224 / CCM 2186 / VKM B-718.
[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: NCIMB 8224 / CCM 2186 / VKM B-718.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06036 Genomic DNA. Translation: AAA22197.1.
PIR	I39766.
3D structure databases
ProteinModelPortal	Q07908.
SMR	Q07908. Positions 6-408.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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]
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_GEOSE

Accession

Primary (citable) accession number: Q07908

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	October 19, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program