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Database: UniProt
Entry: A2QTL8_ASPNC
LinkDB: A2QTL8_ASPNC
Original site: A2QTL8_ASPNC 
ID   A2QTL8_ASPNC            Unreviewed;       548 AA.
AC   A2QTL8;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=An09g02560 {ECO:0000313|EMBL:CAK40193.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40193.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK40193.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270196; CAK40193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QTL8; -.
DR   EnsemblFungi; CAK40193; CAK40193; An09g02560.
DR   VEuPathDB; FungiDB:An09g02560; -.
DR   HOGENOM; CLU_004498_6_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1L.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:UP000006706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..548
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002645078"
FT   DOMAIN          48..489
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   548 AA;  61669 MW;  948B14769761A69E CRC64;
     MHTIPITVSL YAFLATTFLF SCSAYVAQAP LSDDKCTETT VAILGGGMAG IAAAQALSNA
     SIDDFIILEY RDTLGGRVWH TDFGKDKQGK PYVIELGANW LQGLGSEAIE NPVWALAKKY
     RLKNTYSNYS SIRTYNETGY TDYRYLLDEY AQAYHIAARD AGRILTQNLQ DQTARTGLAL
     AGWRPRKNDM AAQAVEWWSW DWEDAHTPET SSLVFGIAGE NLTFNQFGKA NHLVLDPRGY
     STIIQNEALG FLPNPSDGRL RLNTRVTRIE YSPRGVTIHT TNDNNKNSNT CIRAAYAICT
     FSLGVLQNKA VTFDPPLPSW KQTAIEKFNM GTYTKIFMQF PETFWPTDTQ FFLYASPTTR
     GYYPVFQSLS TENFLPESNI LFATVVDEQA YRVERQSLTQ TKDQILNVLR EMFPDKHIPE
     PTAFTYPRWT NEPWVYGSYS NWPAGTTLEM HQNLRANTGR LWFAGEATSA AYFGFLHGAW
     YEGRDAGENV AALLQGRCVE DVSTTSTASG KEEKEEACGE RVFYEQLNGT TPLDAYSRLN
     GWPAVSYY
//
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