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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//