ID A0A1E3PR13_9ASCO Unreviewed; 505 AA.
AC A0A1E3PR13;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:ODQ67684.1};
GN ORFNames=NADFUDRAFT_50103 {ECO:0000313|EMBL:ODQ67684.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ67684.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ67684.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ67684.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KV454407; ODQ67684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PR13; -.
DR STRING; 857566.A0A1E3PR13; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000095009; 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; 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; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 3.
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:UP000095009}.
SQ SEQUENCE 505 AA; 57152 MW; 9B106F5AC9B05F63 CRC64;
MTKFDIDSVA IIGAGPGGLA TLYEFLHTNQ DGISTVGKVR ATHPVFRKIV AFEQKDKAGG
IWATSGNEVD LPIPPQNLLD TGSYTSPDII HPSQSIPENL NQASVHQPFA TDIDRSTSEL
EWKRSGVFPK MFTNIPSRFT RFSYLPNEEK YLDKSRIIYP FLTHKELSQR LVDFTEDEKL
SQYVRVNSRV ESLTKTNGKW VVTVRHTNIE KNKDEWYQEE FDAVVIANGH YTVPNIPHLP
GLAKFNETHP GVLIHSKSYR SSKFFEGKKL LVVGGSISSV NLLQFVVPAA KETFISKRSP
HLVFPWINKA LESEGITTKP TIEKFIPETN EVLFTDGTRE KDFDAILLAT GYHFHYPFLN
NYLNVIEPSN LSRVSGLYYN TFAIKDPTLA TVGVAVSTIN FHTIEASAAA IAGVWSNAKF
LPPKNEQIKW EQVQIDSTAN NLLFHYYTHD KVKEDFIDKL YVYAPDERYN PMEIDAQFLN
DIDEGFAALE NLFYKLKDGV LEITD
//
