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Database: UniProt
Entry: F6ENA6_HOYSD
LinkDB: F6ENA6_HOYSD
Original site: F6ENA6_HOYSD 
ID   F6ENA6_HOYSD            Unreviewed;       502 AA.
AC   F6ENA6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:AEF40377.1};
GN   OrderedLocusNames=AS9A_1928 {ECO:0000313|EMBL:AEF40377.1};
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:AEF40377.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF40377.1, 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; AEF40377.1; -; Genomic_DNA.
DR   RefSeq; WP_013806726.1; NC_015564.1.
DR   AlphaFoldDB; F6ENA6; -.
DR   STRING; 443218.AS9A_1928; -.
DR   KEGG; asd:AS9A_1928; -.
DR   eggNOG; COG2072; Bacteria.
DR   HOGENOM; CLU_006937_7_1_11; -.
DR   OrthoDB; 5168853at2; -.
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; 3.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
SQ   SEQUENCE   502 AA;  56114 MW;  947D1AF652209263 CRC64;
     MSAPNSVGGQ ESHRPLPSHV HILIAGAGFS GLGAAIRLGQ SGMNDYVVVE KAADVGGTWE
     ANSYPGCACD VPSVLYSYSF ARNPHWSSTF SPQPEIYAYL QRTAREFGVM PKVHLRTELL
     DAYWDDAAKR WQITTDRGSL SATIFINATG PLSDVAIPEI PGQEAFVGNA FHSARWDHGY
     DIAGKRVAII GTGASAIQFV PEIQPLVEHF VLFQRTAPWI LPRRDRTYTK LEKRLFRHVP
     FLQRLARYIT YWYRESYVIG FTRIRSALRI AETVGRYNIR RQIKDRELRK KVAPTFQLGC
     KRVLMSNTYY RALDQGNADV NTTGIAQITE NSVIAKDGTE YPVDCIIYGT GFHVSDAAIA
     KNVKGRSGRT LDEVWKGSPE AYLGITVADF PNYFHMVGPN TGLGHSSIVF IIEAQLRYII
     DAIAQLGKRK LAAIEPMPQA QREWVDFVQE KSQGTVWLAG GCDSWYIDEM GRNSTLWPGF
     TFTYRKLTAK ADPEHHIAVA EV
//
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