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Database: UniProt
Entry: A0A1Y5SWF0_9RHOB
LinkDB: A0A1Y5SWF0_9RHOB
Original site: A0A1Y5SWF0_9RHOB 
ID   A0A1Y5SWF0_9RHOB        Unreviewed;       447 AA.
AC   A0A1Y5SWF0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Trimethylamine monooxygenase {ECO:0000256|ARBA:ARBA00035159};
DE            EC=1.14.13.148 {ECO:0000256|ARBA:ARBA00034528};
GN   Name=hapE_2 {ECO:0000313|EMBL:SLN48102.1};
GN   ORFNames=PEL8287_02491 {ECO:0000313|EMBL:SLN48102.1};
OS   Roseovarius litorisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN48102.1, ECO:0000313|Proteomes:UP000193827};
RN   [1] {ECO:0000313|EMBL:SLN48102.1, ECO:0000313|Proteomes:UP000193827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN48102.1,
RC   ECO:0000313|Proteomes:UP000193827};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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}.
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DR   EMBL; FWFL01000006; SLN48102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SWF0; -.
DR   OrthoDB; 9790219at2; -.
DR   Proteomes; UP000193827; Unassembled WGS sequence.
DR   GO; GO:0033767; F:4-hydroxyacetophenone monooxygenase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:SLN48102.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SLN48102.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT   REGION          418..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  51027 MW;  5D3B40A76EAD767A CRC64;
     MAKKKVAIIG AGPSGLAQLR AFQSAAKNGE DIPEIVCFEK QSDWGGLWNY TWRTGVDASG
     EPCHGSMYRY LWSNGPKEGL EFADYTFDEH FGKEIASYPP RAVLFDYIKG RVEKAGVRDW
     IRFNNIVRDV HYNDDTGMFT VTARDTVKDA ETVEDYDHVI VASGHFSTPN VPYYPGFESF
     NGRVLHAHDF RDAREFAGKD ILILGTSYSA EDIGSQCWKY GAKSITVAHR TAPMGYDWPD
     NWQEVPALVK VEGKTAYFKD GTSKDVDAII LCTGYRHHFN FLPDDLRLKT ANRLAAADLY
     KGVVWTKNPK MFYLGMQDQW FTFNMFDAQA WWVRDCIMGK IALPDQATME ADPKRREAEE
     DAIEDDYGAI RYQGAYVQEL IDETDYPSFD VEAANQAFFE WKKHKKKNIM EFRNHGYTSP
     MTGKKAPPHH TPWKDALDDS LESYLQT
//
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