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Database: UniProt
Entry: G3XQ62_ASPNA
LinkDB: G3XQ62_ASPNA
Original site: G3XQ62_ASPNA 
ID   G3XQ62_ASPNA            Unreviewed;       527 AA.
AC   G3XQ62;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_192222 {ECO:0000313|EMBL:EHA27411.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA27411.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA27411.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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:EHA27411.1}.
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DR   EMBL; ACJE01000003; EHA27411.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XQ62; -.
DR   STRING; 380704.G3XQ62; -.
DR   HOGENOM; CLU_004498_6_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..527
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003460344"
FT   DOMAIN          42..474
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHA27411.1"
SQ   SEQUENCE   527 AA;  58966 MW;  7F724E262E2E3957 CRC64;
     SIMQLSLLAL LGALALPSAA VPHARDEGQC KQTTVAILGG GMAGIAAAQT LHNASMDDFM
     ILEYRDTIGG RAWHKPFGQD KDGNPYIIEM GCNWVQGLGT PGGPQNPVWT LAQVYNLSTI
     YSNYSNVSTY NQHGYKDYSH LIDTWDDIYD TAAAQAGVML LDNLQDQTAQ TGLALAGWRP
     KVDDMEAQAV DWWSWDFEDA YTPLESSFIF GVAGQNLTVN GFSDEDNFVI DQRGYSHIIH
     GMASTFLKPN DTRLLLNNHI TNISYSDSGV TVHSSDGSCV RASYAICTFS LGVLQHDAVT
     FTPSLPEWKK EAIEGFTMAT YTKIFLQFNE TFWPEDTQYF LYADPYMRGY YPVFQSLSTE
     GFFPGSNIIF VTVTEQFAWR AERQSDEKTK AEVMEVLRKM FPEKDIPDPI AFMYPRWTLE
     PWAYGSYSNW PPSTTLEMHE NLRANAGRLW FAGEATSPTY FGFLHGAWFE GQAAGLHLSS
     ILNGTCKANT TCKGRKHYET LHGTTPLSDY SFVDGWNGNS FYDFNDD
//
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