Reviewed,
UniProtKB/Swiss-Prot P80695 (AMO_KLEOX)
Last modified
June 16, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Primary amine oxidase EC=1.4.3.21 Alternative name(s): Monamine oxidase Tyramine oxidase | ||||
| Gene names |
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| Organism | Klebsiella oxytoca | ||||
| Taxonomic identifier | 571 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella |
Protein attributes
| Sequence length | 56 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Active on tyramine, tryptamine, beta-phenethylamine and dopamine. |
| Catalytic activity | RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2. |
| Cofactor | Binds 1 copper ion per subunit. Contains 1 topaquinone per subunit By similarity. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Post-translational modification | Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity. |
| Sequence similarities | Belongs to the copper/topaquinone oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Catecholamine metabolism |
| Cellular component | Periplasm |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | TPQ |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | amine oxidase activity Inferred from electronic annotation. Source: EC copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW quinone bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca." Hacisalihoglu A., Jongejan J.A., Duine J.A. Microbiology 143:505-512(1997) [PubMed: 9043125] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 8724 / LMD 72.65. |
Cross-references
3D structure databases | |
|---|---|
| HSSP | HSSP built from PDB template 1OAC based on UniProtKB P46883. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.6. 81705. |
Family and domain databases | |
| InterPro | IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. [Graphical view] |
| Pfam | PF01179. Cu_amine_oxid. 1 hit. [Graphical view] |
| PROSITE | PS01164. COPPER_AMINE_OXID_1. Partial match. PS01165. COPPER_AMINE_OXID_2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMO_KLEOX | ||||||||
| Accession | Primary (citable) accession number: P80695 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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