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Database: UniProt
Entry: A0A2N3N8A2_9PEZI
LinkDB: A0A2N3N8A2_9PEZI
Original site: A0A2N3N8A2_9PEZI 
ID   A0A2N3N8A2_9PEZI        Unreviewed;       569 AA.
AC   A0A2N3N8A2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=jhhlp_005004 {ECO:0000313|EMBL:PKS08617.1};
OS   Lomentospora prolificans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX   NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS08617.1, ECO:0000313|Proteomes:UP000233524};
RN   [1] {ECO:0000313|EMBL:PKS08617.1, ECO:0000313|Proteomes:UP000233524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS08617.1,
RC   ECO:0000313|Proteomes:UP000233524};
RX   PubMed=28963165; DOI=10.1534/g3.117.300107;
RA   Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA   Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT   "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT   prolificans (Formerly Scedosporium prolificans).";
RL   G3 (Bethesda) 7:3831-3836(2017).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKS08617.1}.
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DR   EMBL; NLAX01000095; PKS08617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3N8A2; -.
DR   STRING; 41688.A0A2N3N8A2; -.
DR   VEuPathDB; FungiDB:jhhlp_005004; -.
DR   InParanoid; A0A2N3N8A2; -.
DR   OrthoDB; 5490352at2759; -.
DR   Proteomes; UP000233524; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015328; DUF1965.
DR   PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF09248; DUF1965; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233524};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          17..83
FT                   /note="DUF1965"
FT                   /evidence="ECO:0000259|Pfam:PF09248"
FT   DOMAIN          95..503
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        249
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         249
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   569 AA;  64226 MW;  CE944014ABDCE870 CRC64;
     MWSSYWNNPT SDFGDGTLFP LGLYFKSDIT GRDPSQWKLE GWLYNDIFYE TTEAFREAYF
     SDGFVKNGPN VDGAWAQTDR QGDVFPMDTN SPPVAVAPSG SRYKVDSDRK YVEWMDFSFY
     VGFSRDTGMA LYDIKYKGER VLYELGLQEA LAHYAGNDPV QSGTAYLDSF YGFGPYAFEL
     VQGYDCPSYA TFLNTSFYTS ETTHTHPYSI CLFEFDADYP MQRHSTSSYV SVAKNVYFTV
     RSVSTVGNYD YMFREFAANG TSYTFYLDGA IGVEVRASGY IQSAYFAAND EYGFQIHDFL
     SGSMHDHVLN FKADFDIAGE KNTIQLMSVV PVTTNYTWSG GKTRNTMKVE RSFIESEDES
     RFNWAANGAT QVLVVNQDSP NKYGELRGYR VAPAGGTVHL TVQNSSNLAN AAQWAGYDVQ
     VTKQHDHEQS VAHPYNSQDV YDPPINFDKY FNGESLNQTD LVVWLNLGMH HVPHTGDLPN
     TVFTTAHSSI MFSPVNYLLG NPAAQTVNMV RVDYDDGNTT HVEMFGQKTD TCELDFTPIE
     ADLWGYTGDV VVRKFPFDPN NPFFETDDI
//
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