B7LUN8 (ARGE_ESCF3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylornithine deacetylase
Short name=AO
Short name=Acetylornithinase
EC=3.5.1.16

Alternative name(s):
N-acetylornithinase
Short name=NAO

Gene names

Name:	argE
Ordered Locus Names:	EFER_3806

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
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. HAMAP MF_01108 Glutathione By similarity. HAMAP MF_01108
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. HAMAP MF_01108
Subcellular location	Cytoplasm By similarity HAMAP MF_01108.
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: UniProtKB-KW 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: EC cobalt ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
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_1000137070
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)
	B7LUN8 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 4F898BF65142A711	FASTA	383	42,383
	10 20 30 40 50 60 MKNKLPPFIE IYRALIATPS ISATEEALDQ SNAGLITLLA DWFKDLGFNV EVQPVPGTRN 70 80 90 100 110 120 KFNMLASTGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI 130 140 150 160 170 180 LDTLRDVDVT KLKKPLYILA TADEETSMAG ARYFSETTSL RPDCAIIGEP TSLQPVRAHK 190 200 210 220 230 240 GHISNTIRVM GQSGHSSDPA RGVNAIELMH DAIGHILQLR DTLKERYHYE AFTVPYPTLN 250 260 270 280 290 300 LGHIHGGDAA NRICACCELH MDIRPLPGMT LNDLNGLLNE ALAPVSERWP GRLTVEELHP 310 320 330 340 350 360 PIPGYECPPD HQLVEVVEKL LGTHTEVVNY CTEAPFIQTL CPTLVLGPGS INQAHQPDEY 370 380 LETRFIKPTR ELITQVIHHF CWH

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928158 Genomic DNA. Translation: CAQ91241.1.
RefSeq	YP_002384843.1. NC_011740.1.
3D structure databases
ProteinModelPortal	B7LUN8.
ModBase	Search...
Protein-protein interaction databases
STRING	B7LUN8.
Protein family/group databases
MEROPS	M20.974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000121807; EBESCP00000115570; EBESCG00000121351.
GeneID	7120538.
GenomeReviews	Gene locus EFER_3806 in contig CU928158_GR.
KEGG	efe:EFER_3806.
PATRIC	32131925. VBIEscFer122920_3653.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009680.
HOGENOM	HBG728841.
ProtClustDB	PRK05111.
Enzyme and pathway databases
BioCyc	EFER585054:EFER_3806-MONOMER.
Family and domain databases
HAMAP	MF_01108. ArgE. [Tree]
InterPro	IPR010169. AcOrn-deacetyl. IPR001261. ArgE/DapE_CS. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
KO	K01438.
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
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_ESCF3

Accession

Primary (citable) accession number: B7LUN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program