ID A0A0D2DEV9_9EURO Unreviewed; 480 AA.
AC A0A0D2DEV9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=PV05_01032 {ECO:0000313|EMBL:KIW60847.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW60847.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW60847.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW60847.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KN847317; KIW60847.1; -; Genomic_DNA.
DR RefSeq; XP_013321430.1; XM_013465976.1.
DR AlphaFoldDB; A0A0D2DEV9; -.
DR GeneID; 25322940; -.
DR HOGENOM; CLU_006909_5_2_1; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 3.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 7..42
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 480 AA; 53301 MW; F699A1046F1868E7 CRC64;
MIERVRRVAV IGAGVSGVTT AVHLQAEGLN VTVFERAPVA GGVWVLDPRT PHEPTFPSTK
PSLADSVFYN SIENEDPYLL HAPPGPAYET LTNNVATQFL ELSVNSWPAG TPAFVKHNVI
AEYIQDTSIK TGIHERTLYN TRVKNLSKEG NIWRLETSTW NKTTGKATEK VWEFELVVVA
SGHYHAPRVP DIPGLAEWKE AWPSRIQHSK SYRNPNGFED QTIFLIGGSA SSIDIAREVG
PVAKRVYQST RGGFMDTPES WLPPNGTRVP GIASFGELDD EPSVAAGAIP GKVVLVDGRV
LEDIDRVIVA TGYHFTLPFL PRDFHRDDVP REEADGKVLV TDGTMLHNLH KDIFYIPDPS
LAFTGVPFYT ATFSLFEFQA IAIAAVFSGQ AQMPTWDEMT AQYKERIKEK GHGKPFHTLV
GQDVQYAKGL MEWVNLGRDP STKKVDGYSA EWIAAREEFI KTFWERGSKE NKSTAEEFTA
//
