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Database: UniProt
Entry: V2VTD9_9GAMM
LinkDB: V2VTD9_9GAMM
Original site: V2VTD9_9GAMM 
ID   V2VTD9_9GAMM            Unreviewed;       455 AA.
AC   V2VTD9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Trimethylamine monooxygenase {ECO:0000256|ARBA:ARBA00035159};
DE            EC=1.14.13.148 {ECO:0000256|ARBA:ARBA00034528};
GN   ORFNames=P255_01514 {ECO:0000313|EMBL:ESK51014.1};
OS   Acinetobacter brisouii CIP 110357.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK51014.1, ECO:0000313|Proteomes:UP000018418};
RN   [1] {ECO:0000313|EMBL:ESK51014.1, ECO:0000313|Proteomes:UP000018418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK51014.1,
RC   ECO:0000313|Proteomes:UP000018418};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ESK51014.1}.
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DR   EMBL; AYEU01000006; ESK51014.1; -; Genomic_DNA.
DR   RefSeq; WP_004900819.1; NZ_KI530762.1.
DR   AlphaFoldDB; V2VTD9; -.
DR   STRING; 396323.VH98_05420; -.
DR   PATRIC; fig|1341683.3.peg.1500; -.
DR   HOGENOM; CLU_006909_3_0_6; -.
DR   OrthoDB; 9790219at2; -.
DR   Proteomes; UP000018418; 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; 2.
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:SF301; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 2.
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:UP000018418}.
SQ   SEQUENCE   455 AA;  52576 MW;  69E56D71F6636A94 CRC64;
     MTRVAIIGAG PSGMAQLRAF QSAQAKGADI PEIVCFEKQA DWGGLWNYTW RTGIDENGEP
     VHGSMYRYLW SNGPKEALEF ADYSFDEHFG KPIGSYPPRA VLWDYIKGRV EKANVRRYVR
     FNSAVRHIEF NEQTQQFAVS VHDHNQDVVY TEIFDYVVVA SGHFSTPKVP EYEGFKSFGG
     RILHAHDFRD ALEFKDKTVL VVGSSYSAED IGSQCYKYGA KQIISCYRNS PMGYKWPKNW
     SERQKLLRVD QTHAYFADGT SAEVDAIILC TGYLHHFPFM AESIRLKTDN RLYPLGLYKG
     VVWEKNPKLF YLGMQDQWYT FNMFDAQAWY VRDIILNRMA LPSLSEMQAH TLAWHEEEKT
     LTDAAQMYKF QGDYILELIE ATDYPTFDIE AMRLIFLEWK KHKKEDIMTF RDHIYRSAIT
     GTLAAPHHTP WLDALDDSLE AYLTDTPEVP QKKVG
//
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