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Database: UniProt
Entry: Q4WME0_ASPFU
LinkDB: Q4WME0_ASPFU
Original site: Q4WME0_ASPFU 
ID   Q4WME0_ASPFU            Unreviewed;       354 AA.
AC   Q4WME0;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=FAD dependent oxidoreductase superfamily {ECO:0000313|EMBL:EAL88874.1};
DE            EC=1.4.3.3 {ECO:0000313|EMBL:EAL88874.1};
GN   ORFNames=AFUA_6G10230 {ECO:0000313|EMBL:EAL88874.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88874.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL88874.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000189-1};
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC       {ECO:0000256|ARBA:ARBA00006730}.
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:EAL88874.1}.
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DR   EMBL; AAHF01000006; EAL88874.1; -; Genomic_DNA.
DR   RefSeq; XP_750912.1; XM_745819.1.
DR   AlphaFoldDB; Q4WME0; -.
DR   STRING; 330879.Q4WME0; -.
DR   EnsemblFungi; EAL88874; EAL88874; AFUA_6G10230.
DR   GeneID; 3508217; -.
DR   KEGG; afm:AFUA_6G10230; -.
DR   VEuPathDB; FungiDB:Afu6g10230; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   HOGENOM; CLU_034311_3_0_1; -.
DR   InParanoid; Q4WME0; -.
DR   OMA; TDPTRHM; -.
DR   OrthoDB; 2902754at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF29; FAD DEPENDENT OXIDOREDUCTASE SUPERFAMILY (AFU_ORTHOLOGUE AFUA_6G10230); 1.
DR   Pfam; PF01266; DAO; 1.
DR   PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Oxidoreductase {ECO:0000313|EMBL:EAL88874.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          20..340
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   354 AA;  39414 MW;  8D9F1B963890F238 CRC64;
     MGDCDKNLQM PPVPFSQRPI IILGAGIIGC ATARQLLLNG FRVVVVAEFL PGDQNIFYAS
     AWAGATWHAA GGISSEYRYL QAVTHRHLLK MAQEGPESGV CLVDAREYLE EAPSENSSIW
     GKTVVTNFRE LEPGEYPPNF HCGWSYQTLV TDPTRHLPYL RDQITALGGQ FIRKRVESLQ
     ELYAMFPESS VFINASGLGS KTLTDVRDDK CFPERGQNVF YRTDKCRQMY FRNGKEYTYV
     IPRPLSEGVV LGGVKQPNNL SPEVDIDVAR DEIARAHRLA PEIVPADPPE ESLSYIIGIR
     PSRQGGFRLH SEQLGQRTVL SAYGFGGGGY AFSYGIAEAL LTMLEKCERE NVII
//
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