A7ZUH5 (ARGE_ECO24) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 32.
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 O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331111 [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)
| 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_1000065054 | |||||
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] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000800 Genomic DNA. Translation: ABV20039.1. |
| RefSeq | YP_001465454.1. NC_009801.1. |
3D structure databases | |
| ProteinModelPortal | A7ZUH5. |
| SMR | A7ZUH5. Positions 2-381. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7ZUH5. |
Protein family/group databases | |
| MEROPS | M20.974. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000019215; EBESCP00000018277; EBESCG00000018269. |
| GeneID | 5588158. |
| GenomeReviews | Gene locus EcE24377A_4496 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_4496. |
| NMPDR | fig|331111.3.peg.2110. |
| PATRIC | 18298258. VBIEscCol31211_4717. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0624. |
| GeneTree | EBGT00050000009680. |
| HOGENOM | HBG728841. |
| OMA | DIACAHQ. |
| ProtClustDB | PRK05111. |
Enzyme and pathway databases | |
| BioCyc | ECOL331111:ECE24377A_4496-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_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZUH5 | ||||||||
| 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 |

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