Reviewed, UniProtKB/Swiss-Prot P62058 (ARGJ_CORCT)

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- Recommended name:
            Glutamate N-acetyltransferase alpha chain
    2- Recommended name:
            Glutamate N-acetyltransferase beta chain

Gene names

Name:

argJ

Organism

Corynebacterium crenatum

Taxonomic identifier

168810 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	388 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.
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
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 – 182	182	Glutamate N-acetyltransferase alpha chain By similarity		PRO_0000002155
	Chain	183 – 388	206	Glutamate N-acetyltransferase beta chain By similarity		PRO_0000002156
Sites
	Site	182 – 183	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62058-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 1D1F40C3CA23A433	FASTA	388	39,787
	10 20 30 40 50 60 MAEKGITAPK GFVASATTAG IKASGNPDMA LVVNQGPEFS AAAVFTRNRV FAAPVKVSRE 70 80 90 100 110 120 NVADGQIRAV LYNAGNANAC NGLQGEKDAR ESVSHLAQNL GLEDSDIGVC STGLIGELLP 130 140 150 160 170 180 MDKLNAGIDQ LTAEGALGDN GAAAAKAIMT TDTVDKETVV FADGWTVGGM GKGVGMMAPS 190 200 210 220 230 240 LATMLVCLTT DASVTQEMAQ IALANATAVT FDTLDIDGST STNDTVFLLA SGASGITPTQ 250 260 270 280 290 300 DELNDAVYAA CSDIAAKLQA DAEGVTKRVA VTVVGTTNNE QAINAARTVA RDNLFKCAMF 310 320 330 340 350 360 GSDPNWGRVL AAVGMADADM EPEKISVFFN DKAVCLDSTG APGAREVDLS GADIDVRIDL 370 380 GTSGEGQATV RTTDLSFSYV EINSAYST

References

[1]	Tao W., Chen X., Wang Z., Xu Z. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A.S 1.542.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY509864 Genomic DNA. Translation: AAS90753.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Enzyme and pathway databases
BRENDA	2.3.1.35. 293184.
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_CORCT

Accession

Primary (citable) accession number: P62058

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	June 16, 2009
This is version 32 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)