Reviewed, UniProtKB/Swiss-Prot P23908 (ARGE_ECOLI)

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:	b3957, JW3929

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. 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. HAMAP MF_01108 Glutathione. 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. HAMAP MF_01108
Subcellular location	Cytoplasm Probable 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: HAMAP proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylornithine deacetylase activity Ref.1 Inferred from direct assay. Source: UniProtKB 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_0000185240
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)
	P23908-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: AFE04B99B296540B	FASTA	383	42,347
	10 20 30 40 50 60 MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKDLGFNV EVQPVPGTRN 70 80 90 100 110 120 KFNMLASIGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI 130 140 150 160 170 180 LDALRDVDVT KLKKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK 190 200 210 220 230 240 GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DNLKERYHYE 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and biochemical characterization of the Escherichia coli argE gene product." Meinnel T., Schmitt E., Mechulam Y., Blanquet S. J. Bacteriol. 174:2323-2331(1992) [PubMed: 1551850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related." Boyen A., Charlier D.R.M., Sakanyan V., Mett I., Glansdorff N. Gene 116:1-6(1992) [PubMed: 1628835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	Xiao X.G., Cao K.H. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / DH5-alpha and K12 / JM101 / ATCC 33876 / DSM 3948.
[4]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"The regulatory region of the divergent argECBH operon in Escherichia coli K-12." Piette J., Cunin R., Boyen A., Charlier D.R.M., Crabeel M., van Vliet F., Glansdorff N., Squires C., Squires C.L. Nucleic Acids Res. 10:8031-8048(1982) [PubMed: 6761650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. Strain: K12.
[8]	"IS3 can function as a mobile promoter in E. coli." Charlier D.R.M., Piette J., Glansdorff N. Nucleic Acids Res. 10:5935-5948(1982) [PubMed: 6292860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[9]	"Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase." Javid-Majd F., Blanchard J.S. Biochemistry 39:1285-1293(2000) [PubMed: 10684608] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55417 Genomic DNA. Translation: CAA39076.1. X62807 Genomic DNA. Translation: CAA44625.1. AY330219 Genomic DNA. Translation: AAP92671.1. AY331711 Genomic DNA. Translation: AAP92815.1. U00006 Genomic DNA. Translation: AAC43063.1. U00096 Genomic DNA. Translation: AAC76939.1. AP009048 Genomic DNA. Translation: BAE77354.1. J01587 Genomic DNA. Translation: AAB59145.1. J01589 Genomic DNA. Translation: AAA23484.2.
PIR	B42377.
RefSeq	AP_003853.1. NP_418392.1.
3D structure databases
SMR	P23908. Positions 1-378.
ModBase	Search...
Protein-protein interaction databases
STRING	P23908.
Genome annotation databases
GeneID	948456.
GenomeReviews	Gene locus JW3929 in contig AP009048_GR. Gene locus b3957 in contig U00096_GR.
KEGG	ecj:JW3929. eco:b3957.
Organism-specific databases
EchoBASE	EB1263.
EcoGene	EG11286. argE.
CMR	Search...
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HBG728841.
OMA	ILATCDE.
Enzyme and pathway databases
BioCyc	EcoCyc:ACETYLORNDEACET-MONOMER. ECOL168927:B3957-MONOMER. MetaCyc:ACETYLORNDEACET-MONOMER.
Gene expression databases
Genevestigator	P23908.
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]
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_ECOLI

Accession

Primary (citable) accession number: P23908
Secondary accession number(s): Q2M8Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	December 1, 1992
Last modified:	February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)