Q8X742 (ARGE_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 69.
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 |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 383 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde By similarity. HAMAP MF_01108 |
| 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 – 383 | 383 | Acetylornithine deacetylase HAMAP MF_01108 | PRO_0000185241 | |||||
Sites | |||||||||
| Active site | 82 | 1 | By similarity | ||||||
| Active site | 144 | 1 | Proton acceptor 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] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG59159.1. BA000007 Genomic DNA. Translation: BAB38309.1. |
| PIR | C86087. F91239. |
| RefSeq | NP_290594.1. NC_002655.2. NP_312913.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | Q8X742. |
| SMR | Q8X742. Positions 2-382. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000024754; EBESCP00000023647; EBESCG00000023808. EBESCT00000059236; EBESCP00000057064; EBESCG00000058284. |
| GeneID | 914989. 960175. |
| GenomeReviews | Gene locus Z5515 in contig AE005174_GR. Gene locus ECs4886 in contig BA000007_GR. |
| KEGG | ece:Z5515. ecs:ECs4886. |
| PATRIC | 18359447. VBIEscCol44059_4872. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009680. |
| HOGENOM | HBG728841. |
| OMA | DIACAHQ. |
| ProtClustDB | PRK05111. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4886-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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X742 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with