Reviewed,
UniProtKB/Swiss-Prot Q5E2E4 (ARGE_VIBF1)
Last modified
February 9, 2010.
Version 32.
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 |
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| Organism | Vibrio fischeri (strain ATCC 700601 / ES114) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 312309 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio |
Protein attributes
| Sequence length | 378 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01108 Glutathione By similarity. HAMAP MF_01108 |
| 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. HAMAP MF_01108 |
| 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 |
| 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 – 378 | 378 | Acetylornithine deacetylase HAMAP MF_01108 | PRO_1000065065 | |||||
Sites | |||||||||
| Active site | 78 | 1 | By similarity | ||||||
| Active site | 140 | 1 | 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] | "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners." Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P. Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed: 15703294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000020 Genomic DNA. Translation: AAW86802.1. |
| RefSeq | YP_205690.1. |
3D structure databases | |
| SMR | Q5E2E4. Positions 4-373. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5E2E4. |
Protein family/group databases | |
| MEROPS | M20.974. |
Genome annotation databases | |
| GeneID | 3279490. |
| GenomeReviews | Gene locus VF_2307 in contig CP000020_GR. |
| KEGG | vfi:VF_2307. |
| NMPDR | fig|312309.3.peg.2307. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0624. |
| HOGENOM | HBG728841. |
| OMA | ILATCDE. |
| PhylomeDB | Q5E2E4. |
Enzyme and pathway databases | |
| BioCyc | VFIS312309:VF2307-MONOMER. |
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] |
| 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_VIBF1 | ||||||||
| Accession | Primary (citable) accession number: Q5E2E4 | ||||||||
| 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


