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Database: UniProt
Entry: F4NCQ9_KLUMA
LinkDB: F4NCQ9_KLUMA
Original site: F4NCQ9_KLUMA 
ID   F4NCQ9_KLUMA            Unreviewed;       537 AA.
AC   F4NCQ9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   SubName: Full=Flavin-containing monooxygenase {ECO:0000313|EMBL:CCA89276.1};
GN   Name=FMO1 {ECO:0000313|EMBL:CCA89276.1};
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911 {ECO:0000313|EMBL:CCA89276.1};
RN   [1] {ECO:0000313|EMBL:CCA89276.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 608 {ECO:0000313|EMBL:CCA89276.1};
RX   PubMed=21674230; DOI=10.1007/s10482-011-9606-x;
RA   Lane M.M., Burke N., Karreman R., Wolfe K.H., O'Byrne C.P., Morrissey J.P.;
RT   "Physiological and metabolic diversity in the yeast Kluyveromyces
RT   marxianus.";
RL   Antonie Van Leeuwenhoek 100:507-519(2011).
RN   [2] {ECO:0000313|EMBL:CCA89276.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 608 {ECO:0000313|EMBL:CCA89276.1};
RA   Wolfe K.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; FR854195; CCA89276.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4NCQ9; -.
DR   VEuPathDB; FungiDB:KLMA_30019; -.
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; 4.
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, ECO:0000313|EMBL:CCA89276.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   537 AA;  60422 MW;  BC3F95D548A6A92A CRC64;
     MTQGEKSGTS VAIIGAGAAG LTGLFELLHT KKGGSTSLKY NSDGSLDEQS SINDDPAFGD
     IVVFEQSEKV GGVWNPSFDE ADVIPQELFD TERYDDPTVL RPKTKIPDGF SNQPYAEPLK
     IPISESVEAP IKWNRSGIYK SLFSNVARRY LRNSFIPLNP NEEGKSSSKK NRPIDPFITN
     FEVTDQLLTF VEKYSLLQYV RTNSEVVDVK KSTDGLDQWI VTVRETDTKT GIDKWYSQRF
     DKVVVSNGHY SIPHIPRIEG LSKWNKSAPG SILHSKAFRD ESIFKNKRVV FIGTGLSGID
     ILQYAFPLAK EVIVARTPGK KEIFEWLGRA ACSEGIVVKP RISSVDYENG KTVKFVDGTE
     IQDVDLLVFS TGYHWRYPFL NEDDTGISII NEDGSKKIAT HTSLVDGLFK STFSNKDPSL
     AFIGVLMTQF KWPSFEFEAA IIAAVWSGDA KLPPLEKRLE EHKKRLAETG TNLGYHFFPD
     HEFVRYVNDA KYLLPADRRS EDIFDPTYID EQLESVKVAE KLFHELKENT ISVHETE
//
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