O26284 (ARGJ_METTH) 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:	MTH_182

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	402 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 Reference proteome
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_0000002281
	Chain	189 – 402	214	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000002282
Sites
	Site	188 – 189	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O26284 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: BA7EC486BBB39A29	FASTA	402	42,650
	10 20 30 40 50 60 MYTMELRFIR GGVCAVDGVL AAGCREGKYG VGLIINRGST AAAVFTSNRV RAEPVKLTER 70 80 90 100 110 120 VIADGSISAI VANSGNANCF TGREGMDDAR RMARKVAESL SMDESEVAVA STGVIGRRMP 130 140 150 160 170 180 IDKIEFLIQS AAAQLENSEA ASGALAEAIM TTDTFPKEVA VEFELETGEK ARIGAVAKGS 190 200 210 220 230 240 GMIAPNMATM LSFITTDVDA SSSELTEALR VAVDESFNML IVDGDESTND MVIISSTRTS 250 260 270 280 290 300 GRIDSNFREA LVAVCRELAR MMARDGEGVT KSFQVDVVNA GTHEDAKMAA RAIAGSSLVK 310 320 330 340 350 360 TAIFGADPNW GRIVAAAGYS GAEFDPEEIS VTLESDSESV VIVDHGDILA FEGTEELETA 370 380 390 400 ERVMTSKEIR IIVDLAAGDE SATAYGCDLT YDYVRINAEY TT

References

[1]

"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000666 Genomic DNA. Translation: AAB84688.1.
PIR	C69110.
RefSeq	NP_275325.1. NC_000916.1.
3D structure databases
ProteinModelPortal	O26284.
ModBase	Search...
Protein-protein interaction databases
STRING	O26284.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1470143.
GenomeReviews	Gene locus MTH_182 in contig AE000666_GR.
KEGG	mth:MTH182.
NMPDR	fig|187420.1.peg.180.
Phylogenomic databases
eggNOG	arNOG04939.
HOGENOM	HBG284202.
OMA	GRDPNWG.
PhylomeDB	O26284.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH182-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_METTH

Accession

Primary (citable) accession number: O26284

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program