ID   I3TUU5_TISMK            Unreviewed;       653 AA.
AC   I3TUU5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:AFK56533.1};
GN   OrderedLocusNames=TMO_b0525 {ECO:0000313|EMBL:AFK56533.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM2 {ECO:0000313|EMBL:AFK56533.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56533.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK56533.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM2 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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DR   EMBL; CP003238; AFK56533.1; -; Genomic_DNA.
DR   RefSeq; WP_014753285.1; NC_017966.1.
DR   AlphaFoldDB; I3TUU5; -.
DR   KEGG; tmo:TMO_b0525; -.
DR   PATRIC; fig|1110502.3.peg.4785; -.
DR   HOGENOM; CLU_006937_7_1_5; -.
DR   Proteomes; UP000005258; Plasmid pTM2.
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:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:AFK56533.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:AFK56533.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
SQ   SEQUENCE   653 AA;  72133 MW;  5C23E3876AD040E2 CRC64;
     MADHANRDGA LAGAGDIDQD AAFRVAVAIA NIPTLLMVLV QLTGDTRWLE PPYAPERGRG
     LDDNDDGGLP EDVQAEIRAA ATEAILAWRA GRPVAMPRPD DDLLVRMLSV SMAEEVPAEY
     GEIIASGLGL KAHRLGEPGA VPAGFKVLVI GAGVSGICAA IRLRQRGIAC EVIEKGSDFG
     GTWRENRYPG AGVDTPNHIY SFSFAPHDWT RYFALQGELY GYFRKVARDH GLESCTRFDT
     RVLSALWQAE ARRWAVTVRR PDGAEEVLTA DAVVSAVGVL NTPLVPHIPG LDSFPGPCFH
     TAEWPEDLDV TGKRVALVGN GASAMQVAPA IAPQVGQLTI FARSKQWAAP FPQFGKEMPQ
     PIRFLIANMP LYRLWYRQRL AWTFNDRVHA SLQKDPAWPH PDRALNAVND GHRRAFVKYM
     QQELGDRQDL LEKVLPDYPP FGKRMLLDNG WYRTIARDNV ELITDHMAEV RGSRLVSRGG
     EEREADILVL ATGFKATEFL GSYEVRGRDD QALSEVWNGD DARAYLGTAV PGFPNFFMLL
     GPNVGLGHGG SIISAVELQC DYLLSALDEM FRRGAATIEV RPEIHDDYNR RVDEAHAKMV
     WTHEGMENWY RNSRGRVVAI TPWRNDDFWR MTRTVAPADY VFDGGPAAAG DAA
//