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Database: UniProt
Entry: W6Q4E5_PENRF
LinkDB: W6Q4E5_PENRF
Original site: W6Q4E5_PENRF 
ID   W6Q4E5_PENRF            Unreviewed;       438 AA.
AC   W6Q4E5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=PROQFM164_S01g002855 {ECO:0000313|EMBL:CDM29044.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM29044.1};
RN   [1] {ECO:0000313|EMBL:CDM29044.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM29044.1};
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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; HG792015; CDM29044.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6Q4E5; -.
DR   STRING; 1365484.W6Q4E5; -.
DR   OMA; WKLCHLP; -.
DR   OrthoDB; 981595at2759; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF311; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10180)-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..323
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   438 AA;  48673 MW;  75BBB79E207A494D CRC64;
     MKVVIVGGGL GGLACAIACR REGIDVEILE RSPEVHEVGA GIQIPPNGGR IMCDFGLLPQ
     LLEQGSQVQQ VDFRRYKDGR LLRSMPFGDD ITEEFGAPWI IIHRVDYHRI LLDEAIRLGA
     VLQLGAEVEN IYTEQPAVLL AGGRRISADI VIGADGQMST VRRAILESPH SPVPTGDMAY
     RATFSREQLE SLGDERVNKL CQKIAVTSWL GPEKHTIFYP LRGGNEFNLV LVRPDTLSLD
     SRREQGDIEE MRESYANWDE TLQKLVSCVP SVYKWKLTHL SELESWTKGS VALLGDACHP
     TLPYQAQGAA MAVEDGAVIG KLLGLLQVHY LDPRNSGSDP SISTRSSAQD LTAAVLTLYE
     KCRKARTARN VQGAIMNRKL FHIPDGFLQM IRDFLLGYAG VTRKSDWTWL SSFRQGQTLG
     LDVLEDCQKA FEEWRLTL
//
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