ID   J9SMP2_9ACTN            Unreviewed;       642 AA.
AC   J9SMP2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative flavoprotein involved in K+ transport {ECO:0000313|EMBL:AFR49823.1};
GN   ORFNames=KTR9_3188 {ECO:0000313|EMBL:AFR49823.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49823.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR49823.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR49823.1,
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; AFR49823.1; -; Genomic_DNA.
DR   RefSeq; WP_014927437.1; NC_018581.1.
DR   AlphaFoldDB; J9SMP2; -.
DR   STRING; 337191.KTR9_3188; -.
DR   KEGG; gor:KTR9_3188; -.
DR   PATRIC; fig|337191.3.peg.3542; -.
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; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   642 AA;  71724 MW;  5313C701E74ECEE5 CRC64;
     MTLTITPNPQ LDRETVHSVV SAGNVACLLP VLYQLTGEEK WLSAPYTPRS PRGFEELNDG
     GLPPEIRAEI HDAVTDAVLD WCNGKPPAYP SPSGAELARL MSTAMGESIG AEYSPMVAEQ
     LGFAPYQPVD IGSRIQDSRN DFHVVIVGAG ISGLVCAINL EKAGIPYTIF ERDEHLGGTW
     WANRYPGARV DIPSDLYSFS FHPKNWSEYF ARRDEIFDYV SDVAREHGIV ERVRLRHTVD
     SAVWDDADQR WVLSVTGADG RQHDVGATAL VTAAGLHSTP NIPAYPGISE FTGQIVHSAQ
     WPADVDLTGK RVAVVGSGAS AMQLVVAISE QVQSMTIVQR QPQWITPNEH YFAPSDTAKH
     WLFDNIPFYR GWYRFRLYWL YTERTFAALP VDPDRAAKGK QVSSLNDAFR AHFTAYLEHQ
     LGGDADLIRR TTPDHPPFGK RLLIDNGWFA TLRKSNVELL TDRVERLTPT GIVTADGVAR
     EIDVLILCTG FQQQRFLFPM EIRGREGTSL RESWSDDNGR AYLGITTPGF PNLFFLYGPN
     TNPPGGSYIT IAEAQVRYIV ESISRLVTDD LASIECRPEP YERYNEELDA ANDAMVYAMD
     GVDSYYRNTS GRVVTNSPWP VREYWSRTTH PEPSDFVSTP LR
//