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Database: UniProt
Entry: F6EPB0_HOYSD
LinkDB: F6EPB0_HOYSD
Original site: F6EPB0_HOYSD 
ID   F6EPB0_HOYSD            Unreviewed;       529 AA.
AC   F6EPB0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:AEF41770.1};
GN   OrderedLocusNames=AS9A_3328 {ECO:0000313|EMBL:AEF41770.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41770.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF41770.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; CP002786; AEF41770.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6EPB0; -.
DR   STRING; 443218.AS9A_3328; -.
DR   KEGG; asd:AS9A_3328; -.
DR   eggNOG; COG2072; Bacteria.
DR   HOGENOM; CLU_006937_7_1_11; -.
DR   Proteomes; UP000009235; Chromosome.
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; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:AEF41770.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   REGION          503..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  57724 MW;  1268A4466B30889D CRC64;
     MVIGMTVRSE DSGTKTAARH VDVAVIGSGF SGLGAAIKLK ELGTHSFIVL ERGHEVGGTW
     RDNTYPGAAC DVPSQLYSYS FALGDWSRSF SRQPEIQAYL RKVAEDAGVV ENHLFGCEVQ
     EARWDTASGQ WVIETSAGRV TARFLVSGVG ALCEPALPAI PGIGSFAGQM FHSARWDHSA
     DLKGKRVAII GTGASSIQIV PSIAPEVAQL DVYQRTAPWV LPRFDRPYFG IERWAFRNIP
     GLQRLARAGV YAARETQVVG LAKAPKLMAG LQALAQGMIF AQIRDPELRK KVTPDFRIGC
     KRMLISNAYY PALDRDNVDL VTDGITEVRE NSIVTADGTE REIDALIIAT GFHVTDSPTF
     KGIYGREGRS LAEVFDESGM QGYKGTTVSG FPNLFFLVGP NTGLGHTSMV FMIESQLNYV
     VDALKTIERD NIATFEVREE AQAAFNDELQ AQLAPTVWMT GGCASWYLDK HGNNTTLWPG
     FTFSFRNMLK KFDAENYGIT VMAENPDPTA APADSEPVEA TSTGKKARR
//
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