ID A0A0G4L431_9PEZI Unreviewed; 498 AA.
AC A0A0G4L431;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=BN1708_009524 {ECO:0000313|EMBL:CRJ98987.1}, BN1723_011080
GN {ECO:0000313|EMBL:CRK16746.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK16746.1, ECO:0000313|Proteomes:UP000045706};
RN [1] {ECO:0000313|Proteomes:UP000044602, ECO:0000313|Proteomes:UP000045706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ98987.1}, and VL2
RC {ECO:0000313|EMBL:CRK16746.1};
RA Fogelqvist Johan;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVQH01001225; CRJ98987.1; -; Genomic_DNA.
DR EMBL; CVQI01007224; CRK16746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4L431; -.
DR STRING; 100787.A0A0G4L431; -.
DR OrthoDB; 1923690at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR Proteomes; UP000045706; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; 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:SF313; AMINE OXIDASE; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
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:UP000044602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..498
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007404614"
FT DOMAIN 46..165
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT DOMAIN 205..467
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 54927 MW; 8725891709290964 CRC64;
MASKLLAFLA LAAELRPALA TVLPPRVNAK PQACRKTKVA VLGAGISGIT AAQALSGAGV
DDFLILEHND YIGGRVHHTT FGAKPDGSPY TVELGANWIE GVGGTGPVKN PILEATDKAK
IKSVFSNYSA MFSYDHTGAN DYLHLLDEYD GNFTLATQDA GSILEHDLQD SSMRAQAAEW
WSWDFGVSWP PDESGFQFGI TGDNETFNRF GDERYLATEA RGLNAFVREA ALIFLDGLED
PRLLLNTTVE AVEHSTKGVV VRDRDGGCVE AEYAICTFSV GVLQNDVVEF QPRLPVWKRE
AIEQFQMGTY TKIVLQFNES FWPQDAQFLL YADEDERGWY PVFQNLGAPG FLEGSNILFG
TVVGHQAFRA EQQTDEETKG QILAVLRKMF PDVTVPEPTA FMYPRWGQEE WAFGSYSNWP
VSMTLTKQQN LRANVGRLWF AGEANSAKYY GFMHGAYYEG KDAGERVAAM VRGEPIINED
TAPDGQLKGT RSCMGPSI
//