O42890 (AMOH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 73.
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: Putative primary amine oxidase 1 EC=1.4.3.21 Alternative name(s): Copper amine oxidase 1 | ||
| Gene names |
| ||
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) | ||
| Taxonomic identifier | 284812 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 794 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2. |
| Cofactor | Binds 1 copper ion per subunit By similarity. Contains 1 topaquinone per subunit By similarity. |
| 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 | |
|---|---|
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | TPQ |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | amine metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytosol Inferred from direct assay. Source: GeneDB_Spombe |
| Molecular function | aliphatic-amine oxidase activity Inferred from electronic annotation. Source: EC aminoacetone:oxygen oxidoreductase(deaminating) activityInferred from electronic annotation. Source: EC copper ion bindingInferred from sequence or structural similarity. Source: GeneDB_Spombe phenethylamine:oxygen oxidoreductase (deaminating) activityInferred from electronic annotation. Source: EC primary amine oxidase activityInferred from electronic annotation. Source: EC quinone bindingInferred from electronic annotation. Source: InterPro tryptamine:oxygen oxidoreductase (deaminating) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 794 | 794 | Putative primary amine oxidase 1 | PRO_0000064107 | |||||
Sites | |||||||||
| Active site | 309 | 1 | Proton acceptor By similarity | ||||||
| Active site | 394 | 1 | Schiff-base intermediate with substrate; via topaquinone By similarity | ||||||
| Metal binding | 445 | 1 | Copper By similarity | ||||||
| Metal binding | 447 | 1 | Copper By similarity | ||||||
| Metal binding | 604 | 1 | Copper By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 394 | 1 | 2',4',5'-topaquinone By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU329671 Genomic DNA. Translation: CAB38696.1. |
| PIR | T39367. T39171. T50376. |
| RefSeq | NP_596841.2. NM_001023862.2. |
3D structure databases | |
| ProteinModelPortal | O42890. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O42890. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SPBC1289.16c.1; SPBC1289.16c.1:pep; SPBC1289.16c. |
| GeneID | 2539624. |
| KEGG | spo:SPBC1289.16c. |
Organism-specific databases | |
| GeneDB_Spombe | SPBC1289.16c. |
Phylogenomic databases | |
| eggNOG | fuNOG06311. |
| GeneTree | EFGT00050000002396. |
| HOGENOM | HBG325455. |
| OrthoDB | EOG45MRDH. |
Enzyme and pathway databases | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-004821-MONOMER. |
Gene expression databases | |
| ArrayExpress | O42890. |
Family and domain databases | |
| InterPro | IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. IPR016182. Cu_amine_oxidase_N-reg. IPR015800. Cu_amine_oxidase_N2. IPR015801. Cu_amine_oxidase_N2/3. IPR015802. Cu_amine_oxidase_N3. [Graphical view] |
| Gene3D | G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit. |
| KO | K00276. |
| PANTHER | PTHR10638. CuNH_oxidase. 1 hit. |
| Pfam | PF01179. Cu_amine_oxid. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view] |
| SUPFAM | SSF54416. Cu_amine_oxidase_N-reg. 2 hits. SSF49998. CuNH_oxidase. 1 hit. |
| PROSITE | PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMOH1_SCHPO | ||||||||
| Accession | Primary (citable) accession number: O42890 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with