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Database: UniProt
Entry: W6QPA5_PENRF
LinkDB: W6QPA5_PENRF
Original site: W6QPA5_PENRF 
ID   W6QPA5_PENRF            Unreviewed;       465 AA.
AC   W6QPA5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Flavin monooxygenase-like {ECO:0000313|EMBL:CDM37816.1};
GN   ORFNames=PROQFM164_S07g000164 {ECO:0000313|EMBL:CDM37816.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37816.1};
RN   [1] {ECO:0000313|EMBL:CDM37816.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM37816.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; HG792021; CDM37816.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QPA5; -.
DR   STRING; 1365484.W6QPA5; -.
DR   OMA; LYQHVVW; -.
DR   OrthoDB; 2453855at2759; -.
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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
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, ECO:0000313|EMBL:CDM37816.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   465 AA;  52546 MW;  DF626185C0EF7597 CRC64;
     MVPVKRVAVI GAGPAGAIAI DALAQEKTFD IIRVFERREG PGGCWIGDSS QPPTLRDFAS
     LATRTADPPL PIPQSLPAQT LKSDQPRFTE SSVYPYLETN IDFLPMQFAQ EPFPEERSEL
     SISHHGPETP FRKWDVVRKY VRSLVERRGY SDWVSYNTTV ERVEKVGTEW KVTLRKDGEK
     SDYWWVEWFD AVVVASGHFW VPYIPPIEGL EAFEKTRPGS RVVVVGASVS AADIAVDLVE
     TAKEPVHAIT IGHAANGYFG DEAFNHPKIQ KHPSIERVSN RTVHLTNGNC ITDVDHTIFG
     TGYSWTLPFL PAVPVRNNRV PDLYQHVVWQ KDPTLLFVGA VAAGLTFKVF EWQAVLAARL
     LAGRATLPSV EVMQKWEADR VKARGDGVKF TLIFPDFEDY FETVRHLAGE GEEGKGRKLP
     KFRREWVRAF FEGHERRKAM WKRLNLKSRA ALMNTETTHK EVARL
//
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