ID A0A235G9J9_9NOCA Unreviewed; 456 AA.
AC A0A235G9J9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ORFNames=BDB13_3858 {ECO:0000313|EMBL:OYD70258.1};
OS Rhodococcus sp. OK302.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD70258.1, ECO:0000313|Proteomes:UP000215121};
RN [1] {ECO:0000313|EMBL:OYD70258.1, ECO:0000313|Proteomes:UP000215121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK302 {ECO:0000313|EMBL:OYD70258.1,
RC ECO:0000313|Proteomes:UP000215121};
RA Pelletier D.;
RT "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL Submitted (AUG-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 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:OYD70258.1}.
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DR EMBL; NPJZ01000001; OYD70258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235G9J9; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000215121; 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, ECO:0000313|EMBL:OYD70258.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 456 AA; 52126 MW; 664365DF673CFCC5 CRC64;
MTPKIAILGA GPSGLAQLRA FESARKSGLG AVPDIVCYEK QSDCGGMWNY NWRTGLDQNG
EPVHASMYRY LWSNGPKECL EFADYSFEEH FGHPIPSYPP REVLLEYIMG RVEKSDVRKY
IRFNTAVHGV TYCDETEKFT VTVMDHGRGQ LESNEFDYVI VATGHFSTPN APDFDGLEQF
PGRVLHAHDF RDAREFTGKR LLLVGSSYSA EDIGTQCFKY GAAEVTFSYR TAPMGHDWPD
AFSEVPLLTG LDGNVATFQD GSTREVDAII LCTGYQHHFP FLPDHLKLKT KNRLYPRDIY
KGIFFQDNPK LMYLGMQDQY FTFNMFDAQA WYARDAILGR IALPDRDTRD QNIDEWRGRE
ESLTTASSEI KFQAAYIRDL VDQTDYPEFH VEKQGELFED WKRDKKKDIM GYRNQSYAST
LTGTVAPPLH DDWLDILDDS SEAFLRNSLP TPALQR
//
