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Database: UniProt
Entry: A0A117V2C4_9SPHN
LinkDB: A0A117V2C4_9SPHN
Original site: A0A117V2C4_9SPHN 
ID   A0A117V2C4_9SPHN        Unreviewed;       451 AA.
AC   A0A117V2C4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-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=AQZ50_13515 {ECO:0000313|EMBL:KUR76578.1};
OS   Novosphingobium sp. Fuku2-ISO-50.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR76578.1, ECO:0000313|Proteomes:UP000056630};
RN   [1] {ECO:0000313|EMBL:KUR76578.1, ECO:0000313|Proteomes:UP000056630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR76578.1,
RC   ECO:0000313|Proteomes:UP000056630};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) 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:KUR76578.1}.
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DR   EMBL; LLZR01000018; KUR76578.1; -; Genomic_DNA.
DR   RefSeq; WP_067746990.1; NZ_KQ954294.1.
DR   AlphaFoldDB; A0A117V2C4; -.
DR   STRING; 1739114.AQZ50_13515; -.
DR   OrthoDB; 312624at2; -.
DR   Proteomes; UP000056630; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056630}.
SQ   SEQUENCE   451 AA;  51192 MW;  DBEAB0A0D5BA2A7E CRC64;
     MAKRIAVIGA GASGLAVLRA FQSAKAKGID VPEVVCFEKQ EDWGGLWKYT WRTGLDQYGE
     PVHGSMYRYL WSNGPKECLE FADYSFEEHF GRPIPSYPPR AVLHDYIMGR VEKAGVRPFV
     RFNSPVRWVS WDPETSLFTV RVKDQIADET YEETFDHVIV SSGHFSTPNV PEFEGIETFP
     GRVMHAHDFR SADEFAGKDV LMVGSSYSAE DIGTQCIKYG ANSVTFSYRT NPLPFDWPEQ
     FEQRPLLTKV EGDIAHFIDG TSKKVDGIVL CTGYIHHFPF LPDELRLITH NRLYPGNLWQ
     GVVWQDNPNL FYVGMQDQYF TFNMFDAQAW FVRDLILGKL DLPDAETRAA SIADWQGREE
     AAGTPEEQID FQAAYVSQLI AATDYPTLDT AAVAALFKQW EHDKEADIMG YRDHSYRSVL
     TGTVSPRHHT RWMEALDDSL EAFLATSDAT V
//
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