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Database: UniProt
Entry: A0A372MDK3_9ACTN
LinkDB: A0A372MDK3_9ACTN
Original site: A0A372MDK3_9ACTN 
ID   A0A372MDK3_9ACTN        Unreviewed;       511 AA.
AC   A0A372MDK3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:RFU88670.1};
GN   ORFNames=DY218_00215 {ECO:0000313|EMBL:RFU88670.1};
OS   Streptomyces triticagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU88670.1, ECO:0000313|Proteomes:UP000263094};
RN   [1] {ECO:0000313|EMBL:RFU88670.1, ECO:0000313|Proteomes:UP000263094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU88670.1,
RC   ECO:0000313|Proteomes:UP000263094};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of Actinobacteria from
RT   wheat.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFU88670.1}.
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DR   EMBL; QUAK01000003; RFU88670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372MDK3; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000263094; 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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   511 AA;  56653 MW;  49F781B45858835E CRC64;
     MAEHEREREH VKVAVIGTGF GGLGAAVRLR REGITDFVVL ERAGAVGGTW RDNSYPGCAC
     DVPSHLYSFS FAPNPEWPRT FSGQEHIWKY LEHVADTFGL RPHIRFNSEV KQMRWDNDAL
     HWEIDTSAGS ITAEVVVSAT GPLSDPKVPD IEGLDGFEGK VFHSARWDHD YDLRGKRVAM
     IGTGASAIQI VPAIQAEVER MTLFQRTPPW VMPRADRPIS GAERWLHRQL PFTTSARRGL
     LWGIRELQVQ AFTKRPNELG LVESIAKRNM KRAIKDPALR DKLTPSYRIG CKRILLSNTY
     YPALAQPNVD VVASGLKEVR GNTLVASDGT ETEVDAIIFG TGFHVTDMPI AERVIGADGR
     TLAETWTGGM NSLRGATAAG FPNWMTIIGP NTGLGNSSMI LMIESQLNYM ADYLRQVDVL
     GGRAALDARP TAVQGWNDRV QERMKRTVWN TGGCNSWYLD ENGRNTTIWP GTTTEFRAAT
     RRVDLAEYDV LRPAAQANRA GRPAEKVEAD A
//
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