Phenylethylamine oxidase

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

• Cu cation1 Publication

  <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment inⁱ

  • Ref.2

    "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone."
    Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.
    Biochemistry 36:16116-16133(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, DISULFIDE BOND.
  Note: Binds 1 copper ion per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone."
    Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.
    Biochemistry 36:16116-16133(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, DISULFIDE BOND.
• L-topaquinone1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone."
    Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.
    Biochemistry 36:16116-16133(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, DISULFIDE BOND.
  Note: Contains 1 topaquinone per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.2

    "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone."
    Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.
    Biochemistry 36:16116-16133(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, DISULFIDE BOND.

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• aliphatic-amine oxidase activity Source: UniProtKB-EC
• aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
• copper ion binding Source: InterPro
• phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
• primary amine oxidase activity Source: UniProtKB-EC
• quinone binding Source: InterPro
• tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

GO - Biological processⁱ

• amine metabolic process Source: InterPro

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MTPSTIQTAS PFRLASAGEI SEVQGILRTA GLLGPEKRIA YLGVLDPARG 
        60         70         80         90        100
AGSEAEDRRF RVFIHDVSGA RPQEVTVSVT NGTVISAVEL DTAATGELPV 
       110        120        130        140        150
LEEEFEVVEQ LLATDERWLK ALAARNLDVS KVRVAPLSAG VFEYAEERGR 
       160        170        180        190        200
RILRGLAFVQ DFPEDSAWAH PVDGLVAYVD VVSKEVTRVI DTGVFPVPAE 
       210        220        230        240        250
HGNYTDPELT GPLRTTQKPI SITQPEGPSF TVTGGNHIEW EKWSLDVGFD 
       260        270        280        290        300
VREGVVLHNI AFRDGDRLRP IINRASIAEM VVPYGDPSPI RSWQNYFDTG 
       310        320        330        340        350
EYLVGQYANS LELGCDCLGD ITYLSPVISD AFGNPREIRN GICMHEEDWG 
       360        370        380        390        400
ILAKHSDLWS GINYTRRNRR MVISFFTTIG NYDYGFYWYL YLDGTIEFEA 
       410        420        430        440        450
KATGVVFTSA FPEGGSDNIS QLAPGLGAPF HQHIFSARLD MAIDGFTNRV 
       460        470        480        490        500
EEEDVVRQTM GPGNERGNAF SRKRTVLTRE SEAVREADAR TGRTWIISNP 
       510        520        530        540        550
ESKNRLNEPV GYKLHAHNQP TLLADPGSSI ARRAAFATKD LWVTRYADDE 
       560        570        580        590        600
RYPTGDFVNQ HSGGAGLPSY IAQDRDIDGQ DIVVWHTFGL THFPRVEDWP 
       610        620        630 
IMPVDTVGFK LRPEGFFDRS PVLDVPANPS QSGSHCHG              

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ