Q8FB97 (ARGE_ECOL6) 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:	c4916

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [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)

Function	Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde By similarity. HAMAP MF_01108
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 Probable HAMAP MF_01108.
Sequence similarities	Belongs to the peptidase M20A family. ArgE subfamily.
Sequence caution	The sequence AAN83344.1 differs from that shown. Reason: Erroneous initiation.

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_0000185242
Sites
	Active site	82	1	By similarity
	Active site	144	1	Proton acceptor 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)
	Q8FB97 [UniParc]. Last modified April 23, 2003. Version 2. 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]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN83344.1. Different initiation.
RefSeq	NP_756770.1. NC_004431.1.
3D structure databases
ProteinModelPortal	Q8FB97.
SMR	Q8FB97. Positions 2-381.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000040673; EBESCP00000039022; EBESCG00000039723.
GeneID	1040075.
GenomeReviews	Gene locus c4916 in contig AE014075_GR.
KEGG	ecc:c4916.
PATRIC	18287516. VBIEscCol75197_4616.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009680.
HOGENOM	HBG728841.
OMA	DIACAHQ.
PhylomeDB	Q8FB97.
ProtClustDB	PRK05111.
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_ECOL6

Accession

Primary (citable) accession number: Q8FB97

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	April 23, 2003
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program