The domain within your query sequence starts at position 298 and ends at position 708; the E-value for the Cu_amine_oxid domain shown below is 1.3e-91.

PHVKQANDSRYHLEGNTVIYKDWSFSFQLRPSSGLQILNVHFRNEYIAYEIGVQGAMAVH
REKTPAGELTKTMDLGWSLGTVTHELAPGINCPETATFLDVIHYHGTDGPVRYPRALCLF
EIPTGVPVRPTFNTNSAGKINFFSDVMGHKLVLRATSALYNFDYIWDFIFYTTGTISAKM
HATGYIHTTIYTREGLRETHLLTHQLGHSHTHLVHYRVDLDVAGTNNSFHTLQAKQKNTT
NSSSPRRLVQDVMEKTQYSQERQATFSFGQTLPSFLLFSSPKKDIWGYRRSYRLKIYSTS
EQRLTPETQEDLAFSWAR

Cu_amine_oxid

Cu_amine_oxid
PFAM accession number:PF01179
Interpro abstract (IPR015798):

Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor [(PUBMED:8591028)]: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen [(PUBMED:9048544), (PUBMED:9405045)]. In eukaryotes they have a broader range of functions, including cell differentiation and growth, wound healing, detoxification and cell signalling [(PUBMED:8805580)].

The copper amine oxidases occur as mushroom-shaped homodimers of 70-95 kDa, each monomer containing a copper ion and a covalently bound redox cofactor, topaquinone (TPQ). TPQ is formed by post-translational modification of a conserved tyrosine residue. The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry, and has a dual function in catalysis and TPQ biogenesis. The catalytic domain is the largest of the 3-4 domains found in copper amine oxidases, and consists of a beta sandwich of 18 strands in two sheets. The active site is buried and requires a conformational change to allow the substrate access. The two N-terminal domains share a common structural fold, its core consisting of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the stalk, of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other [(PUBMED:8591028), (PUBMED:10576737)].

This entry represents the C-terminal catalytic domain of copper amine oxidases, and has a super-sandwich fold consisting of 18 beta-strands in 2 sheets [(PUBMED:8591028)]. A domain with a similar structural fold can be found as the third domain in lysyl oxidase PplO [(PUBMED:14690425)].

GO process:oxidation-reduction process (GO:0055114), amine metabolic process (GO:0009308)
GO function:primary amine oxidase activity (GO:0008131), quinone binding (GO:0048038), copper ion binding (GO:0005507)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Cu_amine_oxid