Reviewed, UniProtKB/Swiss-Prot Q7NE46 (ARGJ_GLOVI)

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:	glr4034

Organism

Gloeobacter violaceus [Complete proteome] [HAMAP]

Taxonomic identifier

33072 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Gloeobacteria › Gloeobacterales › Gloeobacter

Protein attributes

Sequence length	406 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 – 190	190	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002171
	Chain	191 – 406	216	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002172
Sites
	Site	190 – 191	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7NE46-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 70714DA5408C2BB6	FASTA	406	41,584
	10 20 30 40 50 60 MADFEWIDGG VTAAKGFRAG GIASGIKPSG KTDLALIYSE NPSAAAGVYT TNLVQAAPVA 70 80 90 100 110 120 YNRNLLQQRG KACAIVVNSG NANAATGKAG EEAAIETAQV FARALGFSAD QVLVASTGVI 130 140 150 160 170 180 GVPLPIEKIR TAAQALVDAA TETGSDAAAE AILTTDLVAK SCAVRALIGG KTVHVGGIAK 190 200 210 220 230 240 GSGMIHPQMA TLLAFITSDC SVDIDLWRQI VARATDRSFN QITVDGDTST NDMLLALASG 250 260 270 280 290 300 EAKNPRILDA ASPEAGLLEQ MVSAVCVDLA KKVVRDGEGA TKLIEVQVAG TGDDAQARKI 310 320 330 340 350 360 ALTVASSSLV KSAMFGNDPN WGRLAAAAGR AGVEFDPAAL AVRLGAFALM EVGQPLAFDR 370 380 390 400 AAASDYLKGS DTVEVHLQVG PGTGNGIAWG CDLSYDYVKI NAEYTT

References

[1]

"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids." Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S. DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7421.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000045 Genomic DNA. Translation: BAC91975.1.
RefSeq	NP_926980.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	2602437.
GenomeReviews	Gene locus glr4034 in contig BA000045_GR.
NMPDR	fig|251221.1.peg.4034.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7NE46.
OMA	Q7NE46. IVNSGNA.
Enzyme and pathway databases
BioCyc	GVIO251221:GLR4034-MON.
BRENDA	2.3.1.1. 276183. 2.3.1.35. 276183.
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_GLOVI

Accession

Primary (citable) accession number: Q7NE46

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 41 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)