A9AB46 (ARGJ_METM6) 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:	MmarC6_1758

Organism

Methanococcus maripaludis (strain C6 / ATCC BAA-1332) [Complete proteome] [HAMAP]

Taxonomic identifier

444158 [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 By similarity 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_1000137058
	Chain	189 – 408	220	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_1000137059
Sites
	Site	188 – 189	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9AB46 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: F97116FF4CB44867	FASTA	408	43,726
	10 20 30 40 50 60 MAENFMVVDG GVVAPKGFKA NGHKDRKYGA ALIYSETDAV AAGVFTTNKV FAHPVALSKD 70 80 90 100 110 120 VLVNNNVFRA IVANSGNANC FTKGGMEDAK ALVKKAADLL KIPENQVLSA STGVIGRRMP 130 140 150 160 170 180 MDIITIEVER AFKNMNLENS NENASKAIMT TDAFPKTVAV EFEINGKNVR IGGIAKGAGM 190 200 210 220 230 240 IAPNMLHATM LGFITTDIEI SKEELTDSLQ KATDESFNNA VVDGDMSTND TVYVLANAQS 250 260 270 280 290 300 GVKYTDCKAD FDGALAYVSK ELAKMIVSDG EGAKKLIEAT VHGAETKEDA KKASMSIVRS 310 320 330 340 350 360 LLLKTAVFGA DPNWGRIAAA VGYSGAEMDM ANFDIIISDI SLENQAFLVK AGEQIADCGT 370 380 390 400 PELKLAEEIM KEDKIKIIVD LKMGSFENTA FGCDLGYEYV RINSEYTT

References

[1]

"Complete sequence of Methanococcus maripaludis C6." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C6 / ATCC BAA-1332.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000867 Genomic DNA. Translation: ABX02569.1.
RefSeq	YP_001549801.1. NC_009975.1.
3D structure databases
ProteinModelPortal	A9AB46.
ModBase	Search...
Protein-protein interaction databases
STRING	A9AB46.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5737502.
GenomeReviews	Gene locus MmarC6_1758 in contig CP000867_GR.
KEGG	mmx:MmarC6_1758.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284202.
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	MMAR444158:MMARC6_1758-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_METM6

Accession

Primary (citable) accession number: A9AB46

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	January 15, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program