B7MR48 (ARGE_ECO81) 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:	ECED1_4662

Organism

Escherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP]

Taxonomic identifier

585397 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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-Rule 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-Rule 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: InterPro metallopeptidase 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-Rule MF_01108		PRO_1000163955
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)
	B7MR48 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: DDD84477F025524E	FASTA	383	42,266
	10 20 30 40 50 60 MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKDLGFNV EVQPVPGTRN 70 80 90 100 110 120 KFNMLASCGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI 130 140 150 160 170 180 LDALRDVDVT KLAKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK 190 200 210 220 230 240 GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DNLKERYHYD AFTVPYPTLN 250 260 270 280 290 300 LGHIHGGDAS NRICACCELH MDIRPLPGMT LNELNGLLND ALAPVSERWP GRLTVDELHP 310 320 330 340 350 360 PIPGYECPPN HQLVEVVEKL LGAKTEVVNY 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ED1a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928162 Genomic DNA. Translation: CAR10632.1.
RefSeq	YP_002400455.1. NC_011745.1.
3D structure databases
ProteinModelPortal	B7MR48.
SMR	B7MR48. Positions 2-381.
ModBase	Search...
Protein-protein interaction databases
STRING	585397.ECED1_4662.
Protein family/group databases
MEROPS	M20.974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR10632; CAR10632; ECED1_4662.
GeneID	7139096.
KEGG	ecq:ECED1_4662.
PATRIC	38493414. VBIEscCol8292_4653.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000243769.
KO	K01438.
OMA	CAHQPGE.
ProtClustDB	PRK05111.
Enzyme and pathway databases
BioCyc	ECOL585397:GJCU-4705-MONOMER.
UniPathway	UPA00068; UER00110.
Family and domain databases
HAMAP	MF_01108. ArgE.
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]
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_ECO81

Accession

Primary (citable) accession number: B7MR48

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program