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Database: UniProt
Entry: A0A0A1YRD9_9PSED
LinkDB: A0A0A1YRD9_9PSED
Original site: A0A0A1YRD9_9PSED 
ID   A0A0A1YRD9_9PSED        Unreviewed;       456 AA.
AC   A0A0A1YRD9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Trimethylamine monooxygenase {ECO:0000256|ARBA:ARBA00035159};
DE            EC=1.14.13.148 {ECO:0000256|ARBA:ARBA00034528};
GN   ORFNames=TMS3_0107265 {ECO:0000313|EMBL:KFX71714.1};
OS   Pseudomonas taeanensis MS-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX71714.1, ECO:0000313|Proteomes:UP000030063};
RN   [1] {ECO:0000313|EMBL:KFX71714.1, ECO:0000313|Proteomes:UP000030063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-3 {ECO:0000313|EMBL:KFX71714.1,
RC   ECO:0000313|Proteomes:UP000030063};
RX   PubMed=24407626;
RA   Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA   Choi J.S., Kahng H.Y., Kim S.I.;
RT   "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT   Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT   Seashore.";
RL   Genome Announc. 2:0-0(2014).
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:KFX71714.1}.
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DR   EMBL; AWSQ01000001; KFX71714.1; -; Genomic_DNA.
DR   RefSeq; WP_025164561.1; NZ_AWSQ01000001.1.
DR   AlphaFoldDB; A0A0A1YRD9; -.
DR   STRING; 1395571.TMS3_0107265; -.
DR   eggNOG; COG2072; Bacteria.
DR   OrthoDB; 9790219at2; -.
DR   Proteomes; UP000030063; 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   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:UP000030063}.
SQ   SEQUENCE   456 AA;  52524 MW;  9D8A7B56BA380AE0 CRC64;
     MKKRVAIIGA GPCGLAQLRA FQSAQDQGAE CPEVVCYEKQ SDWGGMWNYT WRTGLDQHGE
     PVHGSMYRYL WSNGPKECLE FADYSFDEHF GRPLGSYPPR EVLWDYIKGR VEKAGVRKFI
     QFNTAVRGVT YDQNSGLFSV TVHSYDNDQT STEIFDYVVV ASGHFSTPNV PYFEGFESFG
     GRVLHAHDFR DALEFKGKDV LIVGGSYSAE DIGSQCYKYG ARSITSCYRS APMGYRWPDN
     WQEKPLLQRM TGKTAWFADG THHHVDAIIL CTGYKHHFPF LAEELRLKTD NRLWPLSLYK
     GVFWENNLKL IYLGMQDQWY SFNMFDAQAW YARDVILGRI ALPKLAQMQA EDLAWRQEEE
     TLETAQQMFE FQGEYIRQLI EATDYPTFDI SAVNQTFLDW KHDKYEDIMG YRNKCFRSLI
     SGTMATPHHT PWLEALDDSL EAYLSETPAV TQVTAI
//
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