ID A0A1B7M0A0_9MICC Unreviewed; 469 AA.
AC A0A1B7M0A0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Trimethylamine monooxygenase {ECO:0000256|ARBA:ARBA00035159};
DE EC=1.14.13.148 {ECO:0000256|ARBA:ARBA00034528};
GN ORFNames=A6F49_08680 {ECO:0000313|EMBL:OAV61508.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV61508.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV61508.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV61508.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-2016) 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 FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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:OAV61508.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXEY01000016; OAV61508.1; -; Genomic_DNA.
DR RefSeq; WP_043057610.1; NZ_LXEY01000016.1.
DR AlphaFoldDB; A0A1B7M0A0; -.
DR STRING; 1837282.A6F49_08680; -.
DR OrthoDB; 9808049at2; -.
DR Proteomes; UP000078292; 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; 1.
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}.
SQ SEQUENCE 469 AA; 53863 MW; D37930BB2E66FEE9 CRC64;
MQKQRIAIIG AGPSGLAALR AFESAERAGA AIPEIVCYEK QDDWGGQWNY SWRTGIDQYG
EPVHSSMYRN LWSNAPKEAL EFAEYTFDKH FGRPISSYPP REVLWDYIDG RLRSSNARDK
VQFATAARWV QYNEATDTFT VTVEDLKTRT TSSSEFDRVI VATGHFAYPN VPSFEGIETF
PGSVEHAHDF RGAEMLADKR VLMIGSSYSA EDIGVQAYKM GARSVTLSYR SKALGHDWPQ
GMEELPLVQR IEGNSVHFIN GEVREFDSIV MCTGYIHKYP FLPSQLAIDS PNNVYPSGLY
RGVVWQENPK LYYLGAQDQW FTFNMFDAQA WYVRDLILGR TALPSVQDRA AHIESWSKRF
SELSCVDDEV RFQADYIRDL IENSDYPMFD LDSVVEIFIA WQRDKAENVL TYRDKQYRSV
MTGTMSARHH TPWMRELDDS LQRYLSQPEK DEIAKMLDDE DVTESIRAN
//
