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Database: UniProt
Entry: B0YBD2_ASPFC
LinkDB: B0YBD2_ASPFC
Original site: B0YBD2_ASPFC 
ID   B0YBD2_ASPFC            Unreviewed;       697 AA.
AC   B0YBD2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=L-amino acid oxidase LaoA {ECO:0000313|EMBL:EDP48522.1};
GN   ORFNames=AFUB_092390 {ECO:0000313|EMBL:EDP48522.1};
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP48522.1, ECO:0000313|Proteomes:UP000001699};
RN   [1] {ECO:0000313|EMBL:EDP48522.1, ECO:0000313|Proteomes:UP000001699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC   {ECO:0000313|Proteomes:UP000001699};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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DR   EMBL; DS499601; EDP48522.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YBD2; -.
DR   EnsemblFungi; EDP48522; EDP48522; AFUB_092390.
DR   VEuPathDB; FungiDB:AFUB_092390; -.
DR   HOGENOM; CLU_004498_8_2_1; -.
DR   PhylomeDB; B0YBD2; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.240; -; 1.
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   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF418; L-AMINO ACID OXIDASE LAOA (AFU_ORTHOLOGUE AFUA_7G06810); 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..697
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002760827"
FT   DOMAIN          186..668
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   697 AA;  78613 MW;  8CA8F714C26705CB CRC64;
     MAFKTVASAA LLLAQVNCVL TRPQGTNILK VSTSDVVQPG GLANIYLDWR ESYSGIIEAI
     YASCLSPDTS STQIIGRFTV DGHPPQRLAW AVSDDAPTDN CIYVHGTQSD RLEPNLLGKS
     EPVRLSQMVK KRSVADANVP LLKDFDSLGA WFDGVAAIKQ KTATHGGVAS SHSSKDSKIA
     IVGAGISGLA TGLMLDSVGV HNWEIIEASD RVGGRFRTRY VAGTQEWAEM GPMRLPYSVT
     YKHSNETLRY TDHEMTFQLA AILNEMNGND PQWKINFIPW IQHHPNELIA QGTRRHPDGR
     IPTRAEIEAD PSLREAPHMS SAEYLSTKNR MDRILKNETT LKSLQRDVWR AHKLAMEEGL
     DEWSEQAMMR HVFKASLNVT DEIWTSSDYD IFWDELHHNS NLGLDGSSGA LGETTWLCID
     GGFNRLSDAF LPHLGNRLTL NRKVRKLEPI PGPNDTTRTR LSWYPNVTHR TYEFEDYDYT
     IMAVPFTMTR FMDLPNFSSV LSRAISEAGL RFKSACKVAL LFRERFWERG PRPIFGGYSK
     PPSKPVGALY YPVYGHNESR PGLIMHYRGG DWSDRFVSFS DEEHVQTVLD SIVSIHGEQA
     RELYTGDYER LCWLQDEHTA TAWCRPDVEQ HKLYIPAYHV TEHNTIFIGE HTAPTHAWVS
     SSLHSAVRGT VQLLLELGLV DEAKTVNEKW MGRWIRL
//
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