ID A0A1M2W314_TRAPU Unreviewed; 504 AA.
AC A0A1M2W314;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=TRAPUB_9183 {ECO:0000313|EMBL:OJT14241.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT14241.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT14241.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT14241.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|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:OJT14241.1}.
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DR EMBL; MNAD01000311; OJT14241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2W314; -.
DR STRING; 154538.A0A1M2W314; -.
DR OMA; QHVLCAW; -.
DR OrthoDB; 1923690at2759; -.
DR Proteomes; UP000184267; Unassembled WGS sequence.
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 InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF313; POLYAMINE OXIDASE 2; 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:UP000184267};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..504
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013290442"
FT DOMAIN 44..478
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 504 AA; 55325 MW; 995E8887020D7098 CRC64;
MVELPAWLLG VGLVMLALPG ASAVSVDGRA LKKDASVLIL GGGVAGVIAA RTLHEQGITN
FTIVEAKGEL GGRLTSTTFG AKGKEVTLEL GANWVQGTQT DNGPANPIWT LVQKHGLKTH
ENDWTGSIVT YNATGPDDYL DLFDESADAY TNLTITAGTR VDKRLVDATA RTGYSLLGAK
SRTPQAMASE YYQFDWEYAQ TPEESSWIAS SWGNNFTYNT DVGGFGDDNQ MALDPRGFKH
IIQAEAAEFL KPAQLRTNST IKTIKNSDSG VSVVLESGEV LHADYALCTF SLGVLQHDDV
VFEPALPDWK EEAIQSMTMA TYTKVFLQFE EKFWFDTEMA LYADPERGRY PVWQSLDHVN
FLPGSGIVFV TTTGDYSLRI ESLPDEQVQE EVLGVLAAMF PNTTIPAPVA FHFPRWNADP
LFRGSYSNWP SSFFSEHHEN LRANVGERLW FAGEATSQKY FGFLHGAYFE GADVATDMAK
CIKAGGCVGM KHVQEVTNAR PYKI
//
