A6UN66 (ARGJ_METVS) 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:	Mevan_0023

Organism

Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224) [Complete proteome] [HAMAP]

Taxonomic identifier

406327 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	408 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 – 188	188	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_1000065052
	Chain	189 – 408	220	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_1000065053
Sites
	Site	188 – 189	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6UN66 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: A61D103C93F319E3	FASTA	408	43,979
	10 20 30 40 50 60 MAENFRIIDG GVTAPKGFIA NGHKDRKYGV TIIASEVDAV CAGVFTTNKV FAHPVSLSKE 70 80 90 100 110 120 TLKNSDTFRA IIANSGNANC FTKGGMDDAR AFVKKASSLL NIPESQILSA STGVIGRKMA 130 140 150 160 170 180 MDILNREVEK AYESLKLESN NENAAKAIMT TDAFKKTVAV EFNVGEKVVK IGGIAKGAGM 190 200 210 220 230 240 IAPNMLHATM LGFITTDIEI SKEELKNSLQ NAADESFNNA VVDGDMSTND TVFVLANGKS 250 260 270 280 290 300 NVNYRECIEE FDKALLYIST ELAKMIVSDG EGAKKLIEAV LKGAATKEDA KKASMSIVRS 310 320 330 340 350 360 LLLKTAIHGA DPNWGRIAAA VGYSGAEMDM NNFDIIISSI TSGKETYLVK CGEQLADEGT 370 380 390 400 AELKMAQEIM KDSKIRITVD LKKGEFKNTS FGCDLGYEYV RINSEYTT

References

[1]

"Complete sequence of Methanococcus vannielii SB." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. , Sieprawska-Lupa M., Whitman W.B., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SB / ATCC 35089 / DSM 1224.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000742 Genomic DNA. Translation: ABR53938.1.
RefSeq	YP_001322550.1. NC_009634.1.
3D structure databases
ProteinModelPortal	A6UN66.
ModBase	Search...
Protein-protein interaction databases
STRING	A6UN66.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5325785.
GenomeReviews	Gene locus Mevan_0023 in contig CP000742_GR.
KEGG	mvn:Mevan_0023.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04939.
HOGENOM	HBG284202.
OMA	FPKLATR.
ProtClustDB	PRK05388.
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_METVS

Accession

Primary (citable) accession number: A6UN66

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program