Reviewed,
UniProtKB/Swiss-Prot P49250 (AMO_KLEAE)
Last modified
June 16, 2009.
Version 55.
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): Copper amine oxidase Monamine oxidase Tyramine oxidase | ||||
| Gene names |
| ||||
| Organism | Klebsiella aerogenes | ||||
| Taxonomic identifier | 28451 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella |
Protein attributes
| Sequence length | 755 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. |
| Subcellular location | |
| Induction | By tyramine and catecholamines. |
| 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 |
| Domain | Signal |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 30 | 30 | Ref.1 | ||||||
| Chain | 31 – 755 | 725 | Primary amine oxidase | PRO_0000035674 | |||||
Sites | |||||||||
| Active site | 413 | 1 | Proton acceptor By similarity | ||||||
| Active site | 496 | 1 | Schiff-base intermediate with substrate; via topaquinone By similarity | ||||||
| Metal binding | 554 | 1 | Copper Potential | ||||||
| Metal binding | 556 | 1 | Copper Potential | ||||||
| Metal binding | 719 | 1 | Copper Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 496 | 1 | 2',4',5'-topaquinone By similarity | ||||||
Sequences
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References
| [1] | "A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene." Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y. J. Bacteriol. 174:2485-2492(1992) [PubMed: 1556068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-41. Strain: W70. |
Cross-references
Sequence databases | |
|---|---|
| D10208 Genomic DNA. Translation: BAA01060.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OAC based on UniProtKB P46883. |
| SMR | P49250. Positions 35-754. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.6. 366. |
Family and domain databases | |
| InterPro | IPR000269. Cu_amine_oxidase. IPR012854. Cu_amine_oxidase-like_N. IPR015798. Cu_amine_oxidase_C. IPR015800. Cu_amine_oxidase_N2. IPR015801. Cu_amine_oxidase_N2/3. IPR015802. Cu_amine_oxidase_N3. [Graphical view] |
| Gene3D | G3DSA:3.30.457.10. Cu_amine_oxidase-like_N. 1 hit. G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit. |
| PANTHER | PTHR10638. CuNH_oxidase. 1 hit. |
| Pfam | PF01179. Cu_amine_oxid. 1 hit. PF07833. Cu_amine_oxidN1. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view] |
| PROSITE | PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMO_KLEAE | ||||||||
| Accession | Primary (citable) accession number: P49250 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


