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C5A0C3 (ARGE_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:BWG_3625
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [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

proteolysis

Inferred from electronic annotation. Source: InterPro

   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_1000213561

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
C5A0C3 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: AFE04B99B296540B

FASTA38342,347
        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

[1]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001396 Genomic DNA. Translation: ACR61915.1.
RefSeqYP_002928818.1. NC_012759.1.

3D structure databases

ProteinModelPortalC5A0C3.
SMRC5A0C3. Positions 1-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595496.BWG_3625.

Protein family/group databases

MEROPSM20.974.

Proteomic databases

PRIDEC5A0C3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR61915; ACR61915; BWG_3625.
GeneID7954529.
KEGGebw:BWG_3625.
PATRIC18276977. VBIEscCol60876_3962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0624.
HOGENOMHOG000243769.
KOK01438.
OMAGSKINMV.
OrthoDBEOG60651W.
ProtClustDBPRK05111.

Enzyme and pathway databases

BioCycECOL595496:GI18-3773-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_ECOBW
AccessionPrimary (citable) accession number: C5A0C3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 34 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