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Database: UniProt
Entry: L0N8M6_9ORTH
LinkDB: L0N8M6_9ORTH
Original site: L0N8M6_9ORTH 
ID   L0N8M6_9ORTH            Unreviewed;       414 AA.
AC   L0N8M6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   Name=fmoc {ECO:0000313|EMBL:CBX26644.1};
OS   Zonocerus variegatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Pyrgomorphoidea; Pyrgomorphidae; Pyrgomorphinae; Zonocerus.
OX   NCBI_TaxID=907066 {ECO:0000313|EMBL:CBX26644.1};
RN   [1] {ECO:0000313|EMBL:CBX26644.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ober D.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBX26644.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Linzhu W., Till B., Dietrich O.;
RT   "Independent recruitment of a flavin-dependent monooxygenase for safe
RT   accumulation of sequestered pyrrolizidine alkaloids in grasshoppers and
RT   moths.";
RL   Submitted (JAN-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; FR696372; CBX26644.1; -; mRNA.
DR   AlphaFoldDB; L0N8M6; -.
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:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 2.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   2: Evidence at transcript level;
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}.
SQ   SEQUENCE   414 AA;  47940 MW;  3D05B3B22C3C884C CRC64;
     MRRVAVLGAG PSGLVAARYL KDAGFEVTVY ERLHHVGGTW NYTDETWMAE DGRPIYSSMY
     QNLLVNLPKE IMAFPDFPFH DIEESYVPSK EIWKYYNNFC DSFDLRKLIK FHHHVENVRP
     CDSGWLVTVT DLTNMVEHSS EFDAVVVCTG QCWCPLYPNV EGSNNFRGRQ THAHTYRNPD
     SFRNRRVLVV GAGPSGHELA LIISYVAKQV FLSRRELKIV EGLFPDNVTE KPLLTSLTEY
     TAYFSDGSSI DIDDILYCTG YRFRFPFLSP ECGIIADEKR VHPLYMHVLN INNPTMGFIG
     VPPAACFSVL FDLQAQLFTA VLTGRCNLPD AETMRKEEEE ELERQLAAGF QPHFMANRQW
     KYFKQLEDMA GAKPVPLYYM KMFDDVVFDW AKDLQHFRRN NYRIIDNENY KKIY
//
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