Reviewed,
UniProtKB/Swiss-Prot B5QXQ2 (ARGE_SALEP)
Last modified
November 3, 2009.
Version 9.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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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 |
| ||||
| Organism | Salmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 550537 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enteritidis |
Protein attributes
| Sequence length | 383 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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. Glutathione By similarity. |
| 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. |
| Subcellular location | Cytoplasm By similarity. |
| 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 proteolysisInferred 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: HAMAP cobalt ion bindingInferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activityInferred from electronic annotation. Source: InterPro protein dimerization activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred 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_1000137075 | |||||
Sites | |||||||||
| Active site | 82 | 1 | By similarity | ||||||
| Active site | 144 | 1 | 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
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References
| [1] | "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways." Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. Parkhill J.Genome Res. 18:1624-1637(2008) [PubMed: 18583645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM933172 Genomic DNA. Translation: CAR35487.1. | |
| RefSeq | YP_002245961.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 6949972. |
| GenomeReviews | Gene locus SEN3915 in contig AM933172_GR. |
| KEGG | set:SEN3915. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | LIIQVIH. |
Family and domain databases | |
| HAMAP | MF_01108. [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_SALEP | ||||||||
| Accession | Primary (citable) accession number: B5QXQ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


