Reviewed,
UniProtKB/Swiss-Prot Q7X3P1 (SPEB_PROMI)
Last modified
July 28, 2009.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Agmatinase EC=3.5.3.11 Alternative name(s): Agmatine ureohydrolase Short name=AUH | ||
| Gene names |
| ||
| Organism | Proteus mirabilis | ||
| Taxonomic identifier | 584 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus |
Protein attributes
| Sequence length | 306 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the formation of putrescine from agmatine By similarity. |
| Catalytic activity | Agmatine + H2O = putrescine + urea. HAMAP MF_01418 |
| Cofactor | Manganese By similarity. |
| Pathway | Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. HAMAP MF_01418 |
| Disruption phenotype | Cells show a delay in differentiation to swarmer cells and are unable to migrate effectively on agar surfaces. Putrescine restores normal cell differentiation and migration ability. Ref.1 |
| Sequence similarities | Belongs to the arginase family. Agmatinase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis |
| Ligand | Manganese Metal-binding |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Biological process | putrescine biosynthetic process Inferred from electronic annotation. Source: HAMAP spermidine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | agmatinase activity Inferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 306 | 306 | Agmatinase HAMAP MF_01418 | PRO_0000173738 | |||||
Sites | |||||||||
| Metal binding | 128 | 1 | Manganese By similarity | ||||||
| Metal binding | 151 | 1 | Manganese By similarity | ||||||
| Metal binding | 153 | 1 | Manganese By similarity | ||||||
| Metal binding | 155 | 1 | Manganese By similarity | ||||||
| Metal binding | 232 | 1 | Manganese By similarity | ||||||
| Metal binding | 234 | 1 | Manganese By similarity | ||||||
Sequences
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References
| [1] | "Evidence that putrescine acts as an extracellular signal required for swarming in Proteus mirabilis." Sturgill G., Rather P.N. Mol. Microbiol. 51:437-446(2004) [PubMed: 14756784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE. |
Cross-references
Sequence databases | |
|---|---|
| AY298901 Genomic DNA. Translation: AAP55488.1. Different initiation. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.5.3.11. 639. |
Family and domain databases | |
| HAMAP | MF_01418. [Tree] |
| InterPro | IPR005925. Agmatinase. IPR006035. Ureohydrolase. [Graphical view] |
| Gene3D | G3DSA:3.40.800.10. Ureohydrolase. 1 hit. |
| PANTHER | PTHR11358. Ureohydrolase. 1 hit. |
| Pfam | PF00491. Arginase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01230. agmatinase. 1 hit. |
| PROSITE | PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SPEB_PROMI | ||||||||
| Accession | Primary (citable) accession number: Q7X3P1 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


