ID A0A319BHY0_ASPLB Unreviewed; 366 AA.
AC A0A319BHY0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:PYH62948.1};
GN ORFNames=BO96DRAFT_323758 {ECO:0000313|EMBL:PYH62948.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH62948.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH62948.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH62948.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KZ821338; PYH62948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319BHY0; -.
DR OrthoDB; 1422702at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF236; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G12060)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 21..56
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 125..331
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 366 AA; 39919 MW; 74FC5A74249CC78C CRC64;
MTFTPGVGPN GIAPPNSSGI HVIIVGLGVA GLTAAIECYR KGHRVTLFER SPVVKGVEGD
GITIGANGSR VTAKWGDGAV HERMLPLRFL IEKIKVIEYT GYDLGEFELR GYNRGDGYTL
NRGTLVTVMY EHARELGIDI RLNSPVTDYW ETDYEGGVVV HGERIAADCV LCAEGVHSKG
REKITGEQLV SWETGWSAFR GCLNTDAVAA DLATRWALDN AEEYDQTVGW VSDDIHFALW
RGRKGRELFW YCTHENEYAA EEGWDGSIDV VENVLDTIKD WPVRPQLEPL IRKGKGGWMM
VIGDASHAAL PSSGQGASQA IEDGAVLAIA LELSGKEDVP LALSVGMAIR YADRPSRRQC
IPCSNG
//
