P62059 (ARGJ_CORDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate N-acetyltransferase
EC=2.3.1.35

Alternative name(s):
Ornithine acetyltransferase
Ornithine transacetylase
Short name=OATase

Cleaved into the following 2 chains:

1. Glutamate N-acetyltransferase alpha chain
2. Glutamate N-acetyltransferase beta chain

Gene names

Name:	argJ
Ordered Locus Names:	DIP1168

Organism

Corynebacterium diphtheriae [Complete proteome] [HAMAP]

Taxonomic identifier

1717 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + 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
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
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: InterPro 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 – 180	180	Glutamate N-acetyltransferase alpha chain By similarity		PRO_0000002157
	Chain	181 – 386	206	Glutamate N-acetyltransferase beta chain By similarity		PRO_0000002158
Sites
	Site	180 – 181	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62059 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: E20A77F541D8314B	FASTA	386	39,803
	10 20 30 40 50 60 MSSRGVTAPQ GFVAAGATAG IKPSGNKDMA LVVNQGPEFV GAAVFTRNRV VASPVKYTKK 70 80 90 100 110 120 AVANGTLRAV LYNSGNANAC NGVQGDKDVH EIVDYLASKL KVDPLDIAAC STGLIGEPLP 130 140 150 160 170 180 VTMIKAGVDK LIPALGDNGG EAADSIMTTD TVAKETVVKC NGWTLGGMGK GVGMMAPSLA 190 200 210 220 230 240 TMLVCLTTDA CVTQAQAHAA LSKACDVTFN TLDIDGSTST NDTVILLANG ASGITPTESE 250 260 270 280 290 300 FNDAVLQACA DIADQLQADA EGVTKRVRIT VTGTTTDSQA LNAARTLGRD NLFKCAMFGS 310 320 330 340 350 360 DPNWGRVLAA VGMADADMDP DNISVYFNDQ PVCLQSGGTP EARQVDLSGI DIDVRVDLGT 370 380 GGPGKAFVRT TDLSHQYVEI NSAYSS

References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J. Nucleic Acids Res. 31:6516-6523(2003) [PubMed: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248357 Genomic DNA. Translation: CAE49688.1.
RefSeq	NP_939525.1. NC_002935.2.
3D structure databases
ProteinModelPortal	P62059.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2648568.
GenomeReviews	Gene locus DIP1168 in contig BX248353_GR.
KEGG	cdi:DIP1168.
NMPDR	fig|257309.1.peg.1116.
PATRIC	21483523. VBICorDip47633_1150.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284202.
OMA	GRDPNWG.
PhylomeDB	P62059.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	CDIP257309:DIP1168-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_CORDI

Accession

Primary (citable) accession number: P62059

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program