Reviewed, UniProtKB/Swiss-Prot B5RF48 (ARGE_SALG2)

Names and origin

Protein names

Recommended name:
    Acetylornithine deacetylase
      Short name=Acetylornithinase
      Short name=AO
    EC=3.5.1.16
Alternative name(s):
    N-acetylornithinase
      Short name=NAO

Gene names

Name:	argE
Ordered Locus Names:	SG3295

Organism

Salmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP]

Taxonomic identifier

550538 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella gallinarum

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + H2O = acetate + L-ornithine. HAMAP MF_01108
Cofactor	Binds 2 zinc or cobalt ions per subunit By similarity. Glutathione By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1. HAMAP MF_01108
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M20A family. ArgE subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylornithine deacetylase activity Inferred from electronic annotation. Source: HAMAP cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding 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 – 383	383	Acetylornithine deacetylase HAMAP MF_01108		PRO_1000137076
Sites
	Active site	82	1	By similarity
	Active site	144	1	By similarity
	Metal binding	80	1	Cobalt or zinc 1 By similarity
	Metal binding	112	1	Cobalt or zinc 1 By similarity
	Metal binding	112	1	Cobalt or zinc 2 By similarity
	Metal binding	145	1	Cobalt or zinc 2 By similarity
	Metal binding	169	1	Cobalt or zinc 1 By similarity
	Metal binding	355	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B5RF48-1 [UniParc]. Last modified November 4, 2008. Version 1. Checksum: A56BDB11FBDE6475	FASTA	383	42,202
	10 20 30 40 50 60 MKNVLPPFIE IYRALIATPS ISATEESLDQ SNASLITLLA GWFSDLGFNV EVQPVPGTRN 70 80 90 100 110 120 KFNMLASTGH GAGGLLLTGH TDTVPFDDGR WTRDPFTLTE HDNKLYGLGT ADMKGFFAFI 130 140 150 160 170 180 LDALRDVDVT KLKKPLYILA TADEETSMAG ARYFSETTAL RPDCAIIGEP TSLQPIRAHK 190 200 210 220 230 240 GHISNVVRVL GQSGHSSDPA RGVNAIELMH DAIGHIMQLR DSLKARYHYE AFTVPYPTLN 250 260 270 280 290 300 LGHIHGGDAS NRICACCELH MDIRPLPGMT LNDLNGLLND ALAPVSERWP GRLTVAELHP 310 320 330 340 350 360 PIPGYECPPD HQLVEVVEKL LGTKTDVVNY CTEAPFMQTL CPTLVLGPGS INQAHQPDEY 370 380 LETRFIKPTR ELITQVVHHF CWH

References

[1]

"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways." Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J. Genome Res. 18:1624-1637(2008) [PubMed: 18583645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM933173 Genomic DNA. Translation: CAR39091.1.
RefSeq	YP_002228104.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M20.974.
Genome annotation databases
GeneID	6923103.
GenomeReviews	Gene locus SG3295 in contig AM933173_GR.
KEGG	seg:SG3295.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	LIIQVIH.
Family and domain databases
HAMAP	MF_01108. [Tree]
InterPro	IPR010169. AcOrn-deacetyl. IPR001261. ArgE/DapE_CS. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
TIGRFAMs	TIGR01892. AcOrn-deacetyl. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGE_SALG2

Accession

Primary (citable) accession number: B5RF48

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	November 4, 2008
Last modified:	November 3, 2009
This is version 10 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)