ID   V6KL56_9ACTN            Unreviewed;       514 AA.
AC   V6KL56;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=4-hydroxyacetophenone monooxygenase {ECO:0000313|EMBL:EST32935.1};
GN   ORFNames=N566_19745 {ECO:0000313|EMBL:EST32935.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST32935.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST32935.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST32935.1};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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:EST32935.1}.
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DR   EMBL; AWQV01000663; EST32935.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6KL56; -.
DR   STRING; 1380770.N566_19745; -.
DR   PATRIC; fig|1380770.3.peg.3420; -.
DR   HOGENOM; CLU_006937_7_1_11; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000017915; 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   Monooxygenase {ECO:0000313|EMBL:EST32935.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017915}.
SQ   SEQUENCE   514 AA;  56908 MW;  2927D2F7BA09424D CRC64;
     MAAQREYEHV RVAVIGSGFG GLGAAVRLRR AGITDFAVLE RRDAVGGTWR DNSYPGCACD
     VPSHLYSFSF APNPEWPRNF SGQQHIRAYL ERVTDTFGLR EHIRFQHEVL QMTWDTDALH
     WVVETSRSTL TADFVVSATG PLSDPKIPDV PGLDTFEGKV FHSARWDHDY DLRGTRVAMV
     GTGASAIQIV PAIQPTVDRL TVFQRTAPWV MPRVDRKISG LERWMHTRLP ATRAARRQLL
     WIMRELQVGA FTKHPGRLGL VERLASAHMK KAVKDPETRR VLIPDYRIGC KRILLSNSWY
     PALAEPNVDL VPSGLKEVRG NTLVAADGTE TEVDAVVFGT GFHVTDMPIA QRIKGADGAT
     LAEKWTGGME ALRGCTAAGF PNFMTVIGPN TGLGNSSMIL IIEAQLNYMV DYLRQLDTLG
     GTVALDARPS AVHAWNHHVQ DRMKRTVWNT GGCDSWYLDA NGRNTTVWPG TTGEFRRVTR
     RLDLGEYEVL RAHPDAARPA ATAAASGTAH KEAR
//