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Database: UniProt
Entry: A0A0B1SYK1_OESDE
LinkDB: A0A0B1SYK1_OESDE
Original site: A0A0B1SYK1_OESDE 
ID   A0A0B1SYK1_OESDE        Unreviewed;       264 AA.
AC   A0A0B1SYK1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=OESDEN_11959 {ECO:0000313|EMBL:KHJ88250.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Strongyloidea; Chabertiidae; Oesophagostominae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ88250.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ88250.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ88250.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU361177};
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|RuleBase:RU361177}.
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DR   EMBL; KN556202; KHJ88250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1SYK1; -.
DR   Proteomes; UP000053660; 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; 1.
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:SF51; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING]; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361177};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361177};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660}.
SQ   SEQUENCE   264 AA;  30053 MW;  04023FF5DD7EB5A0 CRC64;
     MRVCVVGAGV SGLPAIKACL EENLDVVCYE RTADLGGLWN YRPGQKNIGG TVMATTVVNT
     SKEMMAYSDF PPPEDYPNFM HHSKVNEYLH NYAKHFGLME HIRFNTTVKY ITNEDDGYKV
     ELENGEVEHF DKVILCTGHH AEPKYPQLRD IDKFKGQIMH AYDFRDTKGF EGKNVFLLGI
     GNSALDIAVD LAKVAKSVTV STRRGTWVFN KVAAGGMPYD TLYMTRLYDW LMDAVPWTIA
     NDFMENLVQQ RMDHDLYGLR PNHR
//
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