ID   A0A2B7YAA8_9EURO        Unreviewed;       674 AA.
AC   A0A2B7YAA8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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=AJ79_00758 {ECO:0000313|EMBL:PGH18130.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH18130.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH18130.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH18130.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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}.
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:PGH18130.1}.
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DR   EMBL; PDNB01000006; PGH18130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7YAA8; -.
DR   STRING; 1447875.A0A2B7YAA8; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000223968; 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   PANTHER; PTHR10638:SF33; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
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:UP000223968};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          247..651
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          228..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        403
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         403
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   674 AA;  75786 MW;  FE8D788A0623956B CRC64;
     MAPPHPFDPL SPQEISLAVK YIKDAYPGHN VIFRVVTLAE PSKAQMIPYL QAERLAVSSS
     KPPAVVPRPR RIAHVQFYLG DSSDFREVRV DLGSGERLEE SKLEGKHSYL DETLMQACEK
     ACLADQGVRE AIELLELPEG AVVCVEPWTY GTDGMRDMSR RLIMCYLYMR LSSHGDANHY
     AYPLDLCVEM TDELEVLGIF NLPSGVDDRY TPVTEGVRKF DRSKIHGSSE YHPDLVPDRR
     TSTKPYQVVQ PDGPSFHTDG NLITWEKWRM RVGFNYREGL TLHDITYDGR SVFYRLSLSE
     MFVPYGDSRA PFPRKAAFDL GSNGAGVNAN NLKLGCDCLG NIKYFDAYLH NTFGDPVKFP
     NVICCHEIDD GILWKHTNYR TGNAVVTRSR ILVLQTIITV GNYEYIFAFH FTQDACINYE
     VRATGILSTT PINKGDSVPY GTLVAPGVLA PYHQHLFSLR IDPAIDGYEN SLVVEDSIPM
     PLDDPKIHNP FGIGYTTTKE TIETETPLGT DITKARIFKI INENVRNPVN NMPVGYKLVP
     HYSQMLLAHP SSLHAKRSEF CSHPLWVTRY SDRELYSSGD HTMQSFGGEG IASWIKSRAS
     SPASNVRNQD IVLWHTFGTT HNPRIEDWPV MPAEKMLVSL KPVNFFTGNP AVDVPVSTQE
     KNKSVLVDDG ERNN
//