A5F4Z7 (ARGE_VIBC3) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 33.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acetylornithine deacetylase Short name=AO Short name=Acetylornithinase EC=3.5.1.16 Alternative name(s): N-acetylornithinase Short name=NAO | ||||
| Gene names |
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| Organism | Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 345073 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
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: UniProtKB-KW 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: EC cobalt ion bindingInferred from electronic annotation. Source: InterPro metallopeptidase activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: InterPro |
| 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_1000073029 | |||||
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] | Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395. |
| [2] | "A recalibrated molecular clock and independent origins for the cholera pandemic clones." Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L. PLoS ONE 3:E4053-E4053(2008) [PubMed: 19115014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000627 Genomic DNA. Translation: ABQ20373.1. CP001235 Genomic DNA. Translation: ACP10743.1. |
3D structure databases | |
| ProteinModelPortal | A5F4Z7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5F4Z7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GenomeReviews | Gene locus VC0395_A2221 in contig CP000627_GR. Gene locus VC395_2758 in contig CP001235_GR. |
| KEGG | vco:VC0395_A2221. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0624. |
| HOGENOM | HBG728841. |
| OMA | DIACAHQ. |
| ProtClustDB | PRK05111. |
Enzyme and pathway databases | |
| BioCyc | VCHO345073:VC0395_A2221-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] |
| KO | K01438. |
| Pfam | PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view] |
| SUPFAM | SSF55031. Peptidase_M20_dimer. 1 hit. |
| 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_VIBC3 | ||||||||
| Accession | Primary (citable) accession number: A5F4Z7 Secondary accession number(s): C3LXP3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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