Q82SU1 (ARGJ_NITEU) 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
Ordered Locus Names:	NE2213

Organism

Nitrosomonas europaea [Complete proteome] [HAMAP]

Taxonomic identifier

915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas

Protein attributes

Sequence length	409 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.
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
PTM	Autocatalytic cleavage
Technical term	Complete proteome 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 – 192	192	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_0000002203
	Chain	193 – 409	217	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000002204
Sites
	Site	192 – 193	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82SU1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 853F31CFEA2F6F87	FASTA	409	43,340
	10 20 30 40 50 60 MPVNIPPLLP EQLLPIPGLS LGTAEASIKR PGRKDILVIT LAENTRVAGV FTRNRFCAAP 70 80 90 100 110 120 VTVARSHLTG SLPIRALVIN TGNANAGTGQ SGIDHAHATC ASLARLIGCQ TQQVLPFSTG 130 140 150 160 170 180 VIMEPLPVEK IITHLPQALA NLAPDNWFAA AQAIMTTDIV PKGVSRQIQI NGTTVTITGI 190 200 210 220 230 240 AKGSGMIHPN MATMLGYIAT DAAVTQPLLD DLVRYATDRS FNCVTVDGDT STNDALILMA 250 260 270 280 290 300 TGQAGNTPIT VSTDPAFISL QAAITEVAAL LAQMIVRDGE GATKFITVQV ESGKTREECT 310 320 330 340 350 360 KVAYAIAHSP LIKTACFASD PNLGRILAAI GYAGIEDLDV NLVQLYLGNI LVAEHGGRAA 370 380 390 400 SYREEDGQRI MQAPEITIQV KLNRGNASTT VWTCDLSYDY VKINADYRS

References

[1]

"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea." Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J. J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19718 / NBRC 14298.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL954747 Genomic DNA. Translation: CAD86125.1.
RefSeq	NP_842215.1. NC_004757.1.
3D structure databases
ProteinModelPortal	Q82SU1.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1083178.
GenomeReviews	Gene locus NE2213 in contig AL954747_GR.
KEGG	neu:NE2213.
NMPDR	fig|228410.1.peg.2114.
PATRIC	22715811. VBINitEur56163_2484.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284202.
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	NEUR228410:NE2213-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
KO	K00620.
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_NITEU

Accession

Primary (citable) accession number: Q82SU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program