ID D5VNE2_CAUST Unreviewed; 466 AA.
AC D5VNE2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Flavin-containing monooxygenase FMO {ECO:0000313|EMBL:ADG12015.1};
GN OrderedLocusNames=Cseg_3592 {ECO:0000313|EMBL:ADG12015.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG12015.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; CP002008; ADG12015.1; -; Genomic_DNA.
DR RefSeq; WP_013080661.1; NC_014100.1.
DR AlphaFoldDB; D5VNE2; -.
DR STRING; 509190.Cseg_3592; -.
DR KEGG; cse:Cseg_3592; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006909_8_3_5; -.
DR Proteomes; UP000002629; 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; 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; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:ADG12015.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT REGION 439..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 52026 MW; FDD4916C435E7CEC CRC64;
MATGIPQARL PKACVIGAGC SGFTTIKRLK DHGIPYDCFE MSDEIGGTWY YKNPNGMSAC
YDSLHIDTSK WRLAFEDFPV PKDWPDFPHH AQLFQYFKDY VDHFGLRPTI TFNTRVEKAR
RTADGLWAVT LSSGETRLYD ALFVCNGHHW DPRVPEYPGE FDGPAFHAHA YSDPFDPVDM
RGKNVVVVGM GNSAMDIASE LSQRPIAKTL WVSARRGVWV FPKYLNGKPA DKSALPAWVP
RKLGLALSRS VLKKAIGRME DYGLPKPDHE PLEAHPSVSG EFLTRAGCGD IKFKPAIKAL
EGKRVRFADD SVEDVDAIVF ATGYKISFPF FDDPELLPDA DHRFPLFKRM MKPGIDNLFF
MGLAQPLPTL VNFAEQQAKL AAAYLDGQYA PPPRAEMEKI IARDEARHTG HFYESARHTI
QVDFNVYCAD LKKEIAKGEA RARSQGGKLP VAARAEGKSE TLLAPT
//
