ID   J9SI69_9ACTN            Unreviewed;       646 AA.
AC   J9SI69;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative flavoprotein involved in K+ transport {ECO:0000313|EMBL:AFR48828.1};
GN   ORFNames=KTR9_2191 {ECO:0000313|EMBL:AFR48828.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48828.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR48828.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR48828.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; CP002907; AFR48828.1; -; Genomic_DNA.
DR   RefSeq; WP_014926593.1; NC_018581.1.
DR   AlphaFoldDB; J9SI69; -.
DR   STRING; 337191.KTR9_2191; -.
DR   KEGG; gor:KTR9_2191; -.
DR   PATRIC; fig|337191.3.peg.2489; -.
DR   eggNOG; COG2072; Bacteria.
DR   HOGENOM; CLU_006937_7_1_11; -.
DR   Proteomes; UP000003281; 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:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
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   646 AA;  72116 MW;  EBAC524E1208CA0D CRC64;
     MTSVSLRSTR PHTAEIRAAV ADGNIPTLLA VLVEMTGDRR WMADRYRPTR SRGMDDNSSG
     GLAEDIQQEI HEAVVDALDD WYDRGRPERK PADETLVAAL MSFTAGEQVA PEFAPMMTEI
     VRGDLRGRHL PTLPADLATS IDALVIGAGV AGMLISTQLA AAGVEHTVLE KNDEVGGSWY
     ENHYPGAGVD TPSYLYSISS FDHPWSTHFG KRDEVQGYLQ AFADRHAVRD RVRFGTEVLS
     AAYDTDTQRW TVHVRDRDGH QDTLTARILI SAVGILNRPK LPELPGMAGF TGPIFHSAQW
     PDELDEPGAL TGKRVAIVGS GASAMQIGPA IADRVGSLTI FQRSPQWIAP NDDYFAPVGD
     NVHWLMDNLP GYREWYRARL SWIFNDKVHS TLHVDPDWPE QTASINAVNH GHREFYLRYL
     RSELGDRDDL VDLSTPDYPP FGKRMLLDNG WFRMLRRSNV ELVPHGVERV TPGGLVDGTG
     TAHDFDIIVF ATGFHSDRYL YPMDIVGRSG QNTVEAWGDH DAYAYLGITA PDFPNLFILT
     GPNTALGHGG SFISILEYQV RYVCDAVRAM IENRLGALEV RRDVTDEYND AVDRAHATMV
     WTHPAMTNWY RNPDGRVVAV LPWRIVDYWA RTRTVDLADF LAEPLR
//