Reviewed,
UniProtKB/Swiss-Prot P59601 (ARGE_VIBPA)
Last modified
November 3, 2009.
Version 49.
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 | Vibrio parahaemolyticus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 670 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 378 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. |
| Sequence similarities | Belongs to the peptidase M20A family. ArgE subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis |
| 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: HAMAP |
| 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 – 378 | 378 | Acetylornithine deacetylase HAMAP MF_01108 | PRO_0000185252 | |||||
Sites | |||||||||
| Active site | 78 | 1 | By similarity | ||||||
| Active site | 140 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 76 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 108 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 108 | 1 | Cobalt or zinc 2 By similarity | ||||||
| Metal binding | 141 | 1 | Cobalt or zinc 2 By similarity | ||||||
| Metal binding | 165 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 351 | 1 | Cobalt or zinc 2 By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6. |
Cross-references
Sequence databases | |
|---|---|
| BA000031 Genomic DNA. Translation: BAC61023.1. | |
| RefSeq | NP_799139.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M20.974. |
Genome annotation databases | |
| GeneID | 1190310. |
| GenomeReviews | Gene locus VP2760 in contig BA000031_GR. |
| KEGG | vpa:VP2760. |
| NMPDR | fig|223926.1.peg.2760. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P59601. |
| OMA | QPLMILA. |
Enzyme and pathway databases | |
| BioCyc | VPAR223926:VP2760-MON. |
| BRENDA | 3.5.1.16. 3063. |
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_VIBPA | ||||||||
| Accession | Primary (citable) accession number: P59601 | ||||||||
| 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


