ID Q4WAJ8_ASPFU Unreviewed; 496 AA.
AC Q4WAJ8;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 2.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=FAD dependent oxidoreductase, putative {ECO:0000313|EMBL:EAL84738.2};
DE EC=1.5.3.- {ECO:0000313|EMBL:EAL84738.2};
GN ORFNames=AFUA_7G01560 {ECO:0000313|EMBL:EAL84738.2};
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:EAL84738.2, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL84738.2, 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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:EAL84738.2}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000015; EAL84738.2; -; Genomic_DNA.
DR RefSeq; XP_746776.2; XM_741683.2.
DR AlphaFoldDB; Q4WAJ8; -.
DR EnsemblFungi; EAL84738; EAL84738; AFUA_7G01560.
DR GeneID; 3504211; -.
DR KEGG; afm:AFUA_7G01560; -.
DR VEuPathDB; FungiDB:Afu7g01560; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_0_1; -.
DR InParanoid; Q4WAJ8; -.
DR OMA; THPQDHK; -.
DR OrthoDB; 2446456at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF13; DEPENDENT OXIDOREDUCTASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAL84738.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004246104"
FT DOMAIN 58..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 496 AA; 54856 MW; 1E05FED267B92EBC CRC64;
MTRGQPWRAA VAITVAALAR LSAADICSVI KQQGIEIQKP LSPHYYKDLA NYWSAACGDL
KPTCIATPTS ALEMSAIVKQ LHNFDDLFAV KSGGHMPNNG FASIQDGLLI STENLDQVIY
NPEDQTAIIG PGLTWEDAQK GLDGTGRTLV GGRLGGVGVG GYMLGGGLSF LSSQYGWAAN
NVVNFEVVLA NGTVVNANAK ENTDLFAALK GGGNNFGIVT AYTLQTHPQD HKVWGGNYIF
TADKTPQVLS ALRDFTEHYP DDKAAIIVTC EHGLLIHTWI MFLFYDGPEP PEGVFTNFTA
IGPTDTTKTW DSYYDLLKHN DIFILHGQRY TIATETTPLP NKTVGAEVMQ RYYDHWFNVT
NTVLEVPNML GSIAFQPMPR TITSKAKARG GDLLDFPTDQ DYIIIELDFS YAFAADDGKI
DAANQNLYRG FDNIISDNID KGLLPDVYRP LFLNDAYFRQ DYWGRIRTRE QALQTRIKYD
PDGFFQKRTS GGFRLH
//
