ID   A0A0C2H4Z6_9BILA        Unreviewed;        78 AA.
AC   A0A0C2H4Z6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=ANCDUO_00764 {ECO:0000313|EMBL:KIH68895.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH68895.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH68895.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH68895.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) 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; KN726263; KIH68895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2H4Z6; -.
DR   Proteomes; UP000054047; 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:SF166; 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:UP000054047}.
SQ   SEQUENCE   78 AA;  9277 MW;  222A47B39445DB61 CRC64;
     MKSTVINTSK EMTAYSDFPP EPSMANFMHN TEMYRYLKSY AEHHNLKTYI KFNHKVSNIE
     RSSDYKKTGQ WKVSYEDA
//