ID   A0A1L7XHX6_9HELO        Unreviewed;       783 AA.
AC   A0A1L7XHX6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=PAC_14543 {ECO:0000313|EMBL:CZR64645.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR64645.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR64645.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR64645.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FJOG01000027; CZR64645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7XHX6; -.
DR   STRING; 576137.A0A1L7XHX6; -.
DR   OrthoDB; 5490352at2759; -.
DR   Proteomes; UP000184330; 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; -; 2.
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; IPR015800; Cu_amine_oxidase_N2.
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; PF02727; Cu_amine_oxidN2; 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; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 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:UP000184330};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          64..142
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          234..297
FT                   /note="DUF1965"
FT                   /evidence="ECO:0000259|Pfam:PF09248"
FT   DOMAIN          312..721
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        467
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         467
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   783 AA;  88299 MW;  62C17380FC6E7AAD CRC64;
     MSSSSRPWVK ITGFIAFILV VIAASSPFIK HVKTSFIPSH TSDANAYKAP KNNVWSDLSK
     WEANSVANFL LSSSGLNLTD SAKATSDDNA IKLIELLQPN KSDVLSYLDG SSGPPARWAR
     VVVEQGATKE AHVTNYMVGP LPLDESSVVM PLEFCYSSGR NYALNPMADQ AKLLSFAKSF
     AVGIMDILAE ILSDDQHPFD MKGLGVHPRV NYIVDETLMI WMQLYRTGFN SDATSLLPQG
     IYIQLNASTR NPENWKVLQW YFNNKIYANE TEFRVAMESP DFKKSGLNMD GHWNDIEDFD
     SAPPGREMPS PTMVQPNGAR YRIDKEQNFV SWMGFDFYMS TSSDTGLFLH DIRFNGDSVM
     YEVGMQEALA HYAGDDPMQG GQEFLDSFLY MGLYMYELVP GYDCPAYATF LDTEFHFKDF
     PKTNKNSICI FEYTADYPLQ RHTADKRVSI SRNTYLVVRF VSTVWNYDYT FDYIFYLDGT
     IEVKVRASGF IFGAFWTGGQ ANEDEYGFRV HDAVSTSMHD HVINFKADLD IVGTENTMVR
     VGVEPLTAEY PWDDENTSPR NTMHLTKTIV EKEMGIDWPR NSGELFIVMN QNETNKWGQK
     RGYRVMPGTG VGTPVHLTIL NSTTLGKAAE WAANDLWALK RKDTEPRSSS PLNALTPLDP
     IVDFGKYVDD EDIMQEDLVI WFNLGTHHIP HAGDIPNTLM HTSSSSVMFT PFNFHDRDPS
     IHTRQGVKME TGKKVRHFGG SYDAGVRLRK EDLEPDLSRY QVPVDAGTNH SFVDKLGGPA
     PWN
//