ID A0A0M9VPJ5_9BASI Unreviewed; 478 AA.
AC A0A0M9VPJ5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=Malapachy_3977 {ECO:0000313|EMBL:KOS14332.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS14332.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS14332.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS14332.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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}.
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:KOS14332.1}.
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DR EMBL; LGAV01000004; KOS14332.1; -; Genomic_DNA.
DR RefSeq; XP_017991964.1; XM_018138433.1.
DR AlphaFoldDB; A0A0M9VPJ5; -.
DR STRING; 77020.A0A0M9VPJ5; -.
DR GeneID; 28730309; -.
DR VEuPathDB; FungiDB:Malapachy_3977; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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:UP000037751};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..478
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005839280"
FT DOMAIN 30..477
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 478 AA; 51372 MW; 217DAEC58D348817 CRC64;
MKSFRALFLL SVATTALAAT YDAVVVGAGL SGLNAAKTLA ENNKTFVVLE ARDRVGGRVV
NHYLQTGGEV DMGAEFVGPT HDYVIALAKE LGLELFDTYN KGDNVLYLDD KRSTYAASGL
LGAIPPLDPI SLIQIGILQG KVDDMVSKIN VQAPWDSPNA AEYDSKTADE WLNEQDLTAD
ARKILDVGLV EVLSADATEY SLLYLLTYIA AAGNAQHKGT FERLTQTSPG AQQWRVEGGT
GLLAEGLAKI IGADKIKLGM PVSSIVRGDG DNATYTTTST SGETFESRHV IVAMSPPMAD
HIKFTPALTE DRKQVQSKMK MGSLGKGIAK YETPFWRDSG LTGQAVSDKY STRATFDISP
KNGSSGILMG FIQVAQMREL DNATDAEMTA KITEAFTAYF GDKAKNATEW TFSRWDPAPY
SGGGPVAHAP VNVLYPHGKA LRAPIGNLHF AGTESSDYWV GYMDGALRSG ERVAKEID
//
