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B7MR48 (ARGE_ECO81) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP]
Taxonomic identifier585397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_01108

Glutathione By similarity. HAMAP-Rule MF_01108

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. HAMAP-Rule MF_01108

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01108.

Sequence similarities

Belongs to the peptidase M20A family. ArgE subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandCobalt
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylornithine deacetylase activity

Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 383383Acetylornithine deacetylase HAMAP-Rule MF_01108
PRO_1000163955

Sites

Active site821 By similarity
Active site1441 By similarity
Metal binding801Cobalt or zinc 1 By similarity
Metal binding1121Cobalt or zinc 1 By similarity
Metal binding1121Cobalt or zinc 2 By similarity
Metal binding1451Cobalt or zinc 2 By similarity
Metal binding1691Cobalt or zinc 1 By similarity
Metal binding3551Cobalt or zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B7MR48 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: DDD84477F025524E

FASTA38342,266
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928162 Genomic DNA. Translation: CAR10632.1.
RefSeqYP_002400455.1. NC_011745.1.

3D structure databases

ProteinModelPortalB7MR48.
SMRB7MR48. Positions 2-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585397.ECED1_4662.

Protein family/group databases

MEROPSM20.974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR10632; CAR10632; ECED1_4662.
GeneID7139096.
KEGGecq:ECED1_4662.
PATRIC38493414. VBIEscCol8292_4653.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243769.
KOK01438.
OMACETQQIA.
OrthoDBEOG60651W.

Enzyme and pathway databases

BioCycECOL585397:GJCU-4705-MONOMER.
UniPathwayUPA00068; UER00110.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
HAMAPMF_01108. ArgE.
InterProIPR010169. AcOrn-deacetyl.
IPR001261. ArgE/DapE_CS.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01892. AcOrn-deacetyl. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGE_ECO81
AccessionPrimary (citable) accession number: B7MR48
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways