Reviewed, UniProtKB/Swiss-Prot Q9RTQ2 (ARGJ_DEIRA)

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:	DR_1704

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	389 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 – 183	183	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002163
	Chain	184 – 389	206	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002164
Sites
	Site	183 – 184	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RTQ2-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 96A32AC4CCFB8EDE	FASTA	389	39,724
	10 20 30 40 50 60 MTEPLPDVTF PQGFRAAAMA AGIKPSGKPD LSCVVSERDC AWAFAGTRST TAAACVTRNR 70 80 90 100 110 120 ELYASGAPLR ALVVNAGVAN AATGQQGARD NADMADALAS VLAVGEAEVI TASTGVIGHL 130 140 150 160 170 180 LPMDKVLSGV EHLPEELEGA ALPFATAIMT TDTRSKLAHV TLSNGARIVG TAKGSGMIHP 190 200 210 220 230 240 DMATMFAFAF TDAQVDQGAL RGAFPAIVAR TFNAVTVDGD TSTNDMTAVL ANGAAGETDL 250 260 270 280 290 300 TEFLTALEGV MRDLARQIAA DGEGATRLLT VRVTGAASEA EALGAARTCC VSPLLKSAVH 310 320 330 340 350 360 GADPNWGRVI MAVGRSGAGV KVEAMKVSVQ GVPVFAGGPL NYDAAAVSQS MKTDEVIFDV 370 380 DLGVGSARGE AWGCDLSAEY VSINADYTT

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000513 Genomic DNA. Translation: AAF11262.1.
PIR	B75363.
RefSeq	NP_295427.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1799714.
GenomeReviews	Gene locus DR_1704 in contig AE000513_GR.
KEGG	dra:DR_1704.
NMPDR	fig|243230.1.peg.1886.
TIGR	DR_1704.
Phylogenomic databases
HOGENOM	Q9RTQ2.
OMA	IVNSGNA.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1704-MON.
BRENDA	2.3.1.1. 96172. 2.3.1.35. 96172.
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_DEIRA

Accession

Primary (citable) accession number: Q9RTQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 59 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)