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
//