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Database: UniProt
Entry: A0A0M8TT79_9ACTN
LinkDB: A0A0M8TT79_9ACTN
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ID   A0A0M8TT79_9ACTN        Unreviewed;       431 AA.
AC   A0A0M8TT79;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=F420H2:quinone oxidoreductase {ECO:0000313|EMBL:KOU66917.1};
GN   ORFNames=ADK57_18105 {ECO:0000313|EMBL:KOU66917.1};
OS   Streptomyces sp. MMG1533.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU66917.1, ECO:0000313|Proteomes:UP000037741};
RN   [1] {ECO:0000313|Proteomes:UP000037741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:KOU66917.1}.
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DR   EMBL; LGDG01000167; KOU66917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8TT79; -.
DR   STRING; 1415546.ADK57_18105; -.
DR   PATRIC; fig|1415546.3.peg.3934; -.
DR   Proteomes; UP000037741; 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; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
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:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037741}.
SQ   SEQUENCE   431 AA;  47737 MW;  B835E8361F7025E6 CRC64;
     MAVARALAER NLPYTHLERH TGPGGIWDID NPGSPMYESA HFISSRTLSG FGGFPMPDHF
     ADYPPHRQIL SYLRSFADAY GLTDRIEFGV EVENVEKNAD GTWTVTRADG RESVHGQVVV
     CTGSQWHPNI PELPGEFSGE VRHTVGYRSA EEMRGKRVLV VGAGNSGCDI ACDAARTADH
     AVISMRRGYW FIPKHLFGRP VDTIAGSGPH LPMWLAQRVF GALLRIINGD PTRLGLPKPD
     HKLFETHPAI NSMLIHHLQH GDITARPGIA RTEGRSVYFT DGTSDDFDLV LLATGYVHKV
     PVAQRYFGDE QHPDLYLSSF SREHEGLFGI GFIETNSGAY QLFDSQAQLI AGYIHDARHR
     LPNAERFARM IRTDRPDLSG GLKFVDSPRH TGYVDGAAFV KYLGKVAGEM GWRTEGRAPR
     VRSLRPAEAT A
//
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