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Database: UniProt
Entry: G2XBB3_VERDV
LinkDB: G2XBB3_VERDV
Original site: G2XBB3_VERDV 
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
//
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