Acetylornithine deacetylase - Escherichia coli (strain K12)

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P23908 (ARGE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b3957, JW3929

Organism

Escherichia coli (strain K12)

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. Glutathione.
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.
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 Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from direct assay Ref.9. Source: EcoCyc proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylornithine deacetylase activity Inferred from direct assay Ref.1. Source: EcoliWiki cobalt ion binding Inferred from direct assay Ref.9. Source: EcoCyc metallopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.9. Source: EcoCyc
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

By similarity

Active site

144

Proton acceptor By similarity

Metal binding

Cobalt or zinc 1 By similarity

Metal binding

112

Cobalt or zinc 1 By similarity

Metal binding

112

Cobalt or zinc 2 By similarity

Metal binding

145

Cobalt or zinc 2 By similarity

Metal binding

169

Cobalt or zinc 1 By similarity

Metal binding

355

Cobalt or zinc 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P23908 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: AFE04B99B296540B
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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

« Hide

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 / NCIMB 11926.
[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	NP_418392.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P23908.
SMR	P23908. Positions 6-381.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000417; EBESCP00000000417; EBESCG00000000345. EBESCT00000000418; EBESCP00000000418; EBESCG00000000345. EBESCT00000015686; EBESCP00000014977; EBESCG00000014746.
GeneID	948456.
GenomeReviews	Gene locus JW3929 in contig AP009048_GR. Gene locus b3957 in contig U00096_GR.
KEGG	ecj:JW3929. eco:b3957.
PATRIC	32123435. VBIEscCol129921_4078.
Organism-specific databases
EchoBASE	EB1263.
EcoGene	EG11286. argE.
Phylogenomic databases
eggNOG	COG0624.
GeneTree	EBGT00050000009680.
HOGENOM	HBG728841.
OMA	DIACAHQ.
PhylomeDB	P23908.
ProtClustDB	PRK05111.
Enzyme and pathway databases
BioCyc	EcoCyc:ACETYLORNDEACET-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]
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_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:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents