ID G2XBB3_VERDV Unreviewed; 518 AA.
AC G2XBB3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=VDAG_07251 {ECO:0000313|EMBL:EGY16087.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY16087.1};
RN [1] {ECO:0000313|EMBL:EGY16087.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY16087.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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; DS572710; EGY16087.1; -; Genomic_DNA.
DR RefSeq; XP_009654451.1; XM_009656156.1.
DR AlphaFoldDB; G2XBB3; -.
DR STRING; 498257.G2XBB3; -.
DR EnsemblFungi; EGY16087; EGY16087; VDAG_07251.
DR GeneID; 20708714; -.
DR KEGG; vda:VDAG_07251; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_3_1; -.
DR InParanoid; G2XBB3; -.
DR OMA; GETAYEW; -.
DR OrthoDB; 5471885at2759; -.
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 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..518
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003439130"
FT DOMAIN 66..508
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 56697 MW; C16BCE086CCA177A CRC64;
MYTKHGARLL LSVSLLLRAV LGVAAVQVSR PWTPADGHLG DSSNGCDQSP PLPPSEVDVI
VVGGGFSGLT AAYELQQSGY TTLVLEATHL LGGKSRSQRL KIGPGIAELG ATWINNKTQK
TVYEYSQRFG FDTVVQYNDG DTIFQGEDGR VTRSTPSDDS EPEDSELALQ EAAWSLLIEE
SAAKIDISDW DSFPEKKDVS FADWLDIYKM WEKPHLRALS RGLSRAIVGR EPEDIGAHYF
LDYIKSGGGL RSLMFEDQEG AQFQWIKQGT TAIATSLAEA MTPGSVLIYS PVHSVVQQSD
MSIVTIESGQ SFRANKVIIA VTQNVYNKIT FSPPLPCDKR NLVSHTKPGI YAKMALTYSN
SWWRDAGLVG KFTSLAGPAC FGWEISDASQ DLHALMVFIA GSIAEKWGAL PADEKETAVI
EHLAEIFGKE LANEARDVRE VQYVEWTTEE YFLGGPTTTL GAGMLRKYGA VMREPFENLH
FAGTETAFEW KGYLEGAVTA GQRAAQEVVD GLTEIKEA
//