ID A0A0D2JPC5_9EURO Unreviewed; 477 AA.
AC A0A0D2JPC5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=Z520_09128 {ECO:0000313|EMBL:KIX95212.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX95212.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX95212.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX95212.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN848083; KIX95212.1; -; Genomic_DNA.
DR RefSeq; XP_016629335.1; XM_016779624.1.
DR AlphaFoldDB; A0A0D2JPC5; -.
DR STRING; 1442371.A0A0D2JPC5; -.
DR GeneID; 27714874; -.
DR VEuPathDB; FungiDB:Z520_09128; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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:SF1; FLAVIN-CONTAINING MONOAMINE OXIDASE B-RELATED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
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:UP000053411}.
FT DOMAIN 49..461
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 477 AA; 53563 MW; 9428F4FAA796946D CRC64;
MAKSRDGWQW TRREGVKAGL PCIGVINPSQ SVKNLDKVFD IVIIGAGYTG LTAARDLTVA
GFQTLLLEGR DRVGGRTWSS EIDGYQFELG GAWVHWFQPH VYREISRYGM KAELVFSPDY
TREKNYFTFV TEHGARKMSH QEEIELFSRA LEKFANVDGN LGKSVVPLPF DQYSNETLNN
YANMSVADRL EQIKNDLTDD ERNAVSAVVL VAAVAPETIR RSWTFFVVLA IKLECGQSAF
ALRFFQEALS SGRLSYSFNT VITRVDSSSR DIVKVLSRDG LTFRAKRVIC TAPLNVLDKV
RFHPALSQAK LDAIRHKHVN QCTKLHAEIK DPEMRSWGGV TYPNNRLLLG AADGTTPSGN
THCVFFGCSE SHLHAEEEIE ETLKAVNAFA EMEVERLVSH NWSKDQFAEG AWVWYQPGAE
VKYLETLRER HGPILFANSD WADGGWRSFI DGAIQSGTDA AFTVKNELQG AQRESHL
//
