ID A0A1F8A1C0_9EURO Unreviewed; 459 AA.
AC A0A1F8A1C0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=ABOM_006622 {ECO:0000313|EMBL:OGM45125.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM45125.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM45125.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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:OGM45125.1}.
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DR EMBL; LYCR01000046; OGM45125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A1C0; -.
DR STRING; 109264.A0A1F8A1C0; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT DOMAIN 11..448
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 459 AA; 50962 MW; 4F691A1DA4D289DD CRC64;
MFDVVIIGAG LSGLQAAYSA KKAGLKVVVV EARNRVGGKV WTVPLASGRG YADLGAAWIN
DELQKRVTAY ARQFGLKTTK QRLEGKAVMQ LSGDERFEFP FGITPKFSPE ETKNLEYIRD
HIQAKSLRSE PPLPEDDNVT IEQYLLKLGA GPKTLAMVNV WAKAMHGLEI DQYSAAWFID
YCRTNGGLLS VRADDHTGGN YMRFEKGAQQ VPNGLAKLIG EEDIRLNEPV ASIQDHQDHV
TVTTTTGNTY TARKCILSIP STLYKDLNIF PKLPLPVQDV TNNTVLGHYN KSIVCYNTPW
WRKKGFNGFF VSYGGGPVAI ARDSSVDEIG YYSLTCFVNG RPGEKWGNSY PHERRAAVLN
QLAAIFDAEP DSELWRPLEI FEQVWQHERY SKGALAPVHA LGHYTKYAAF YGKPVGNLHF
VGTEYSREWK GYMEGALCSG EIGAQEVIDA LKQGPTAKL
//