Reviewed,
UniProtKB/Swiss-Prot Q9P7F2 (AMOH2_SCHPO)
Last modified
June 16, 2009.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative primary amine oxidase 2 EC=1.4.3.21 Alternative name(s): Copper amine oxidase 2 | ||
| Gene names |
| ||
| Organism | Schizosaccharomyces pombe (Fission yeast) [Complete proteome] | ||
| Taxonomic identifier | 4896 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 712 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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 | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | TPQ |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | amine catabolic process Inferred from direct assay. Source: GeneDB_SPombe copper ion homeostasisInferred from mutant phenotype. Source: GeneDB_SPombe oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe |
| Molecular function | amine oxidase activity Inferred from direct assay. Source: GeneDB_SPombe copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: GeneDB_SPombe 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 712 | 712 | Putative primary amine oxidase 2 | PRO_0000316036 | |||||
Sites | |||||||||
| Active site | 321 | 1 | Proton acceptor By similarity | ||||||
| Active site | 407 | 1 | Schiff-base intermediate with substrate; via topaquinone By similarity | ||||||
| Metal binding | 458 | 1 | Copper By similarity | ||||||
| Metal binding | 460 | 1 | Copper By similarity | ||||||
| Metal binding | 627 | 1 | Copper By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 407 | 1 | 2',4',5'-topaquinone By similarity | ||||||
Sequences
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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: ATCC 38366 / 972. |
| [2] | "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
Cross-references
Sequence databases | |
|---|---|
| CU329670 Genomic DNA. Translation: CAB83008.1. | |
| RefSeq | NP_593985.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EKM based on UniProtKB P12807. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2541754. |
| KEGG | spo:SPAC2E1P3.04. |
| NMPDR | fig|4896.1.peg.3955. |
Organism-specific databases | |
| GeneDB_Spombe | SPAC2E1P3.04. |
Phylogenomic databases | |
| OMA | Q9P7F2. ITHFPAP. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.6. 653. |
Gene expression databases | |
| ArrayExpress | Q9P7F2. |
Family and domain databases | |
| InterPro | IPR000269. Cu_amine_oxidase. 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:3.10.450.40. 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. 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 | AMOH2_SCHPO | ||||||||
| Accession | Primary (citable) accession number: Q9P7F2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


