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Database: UniProt
Entry: A0A059C0W9_EUCGR
LinkDB: A0A059C0W9_EUCGR
Original site: A0A059C0W9_EUCGR 
ID   A0A059C0W9_EUCGR        Unreviewed;       451 AA.
AC   A0A059C0W9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=EUGRSUZ_E00454 {ECO:0000313|EMBL:KCW72002.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW72002.1};
RN   [1] {ECO:0000313|EMBL:KCW72002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW72002.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-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; KK198757; KCW72002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059C0W9; -.
DR   EnsemblPlants; KCW72002; KCW72002; EUGRSUZ_E00454.
DR   Gramene; KCW72002; KCW72002; EUGRSUZ_E00454.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; A0A059C0W9; -.
DR   OMA; YFRYATQ; -.
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   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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361177}.
SQ   SEQUENCE   451 AA;  50930 MW;  35798CF16712D439 CRC64;
     MVSQHVAVIG AGAAGLVAAR ELHHEGHRVV VFERGSCVGG TWVYTPVTEP DPLGIDPSRP
     VVHSSLYKSL RTNLPREVMG FGDYPFLPRE DGSGDPRRYP GHEEVLAYLE DFTREFGLEE
     VVKFEKEIAG VRKAEEEEEG GKWKVAWTMR NDGGGGGGRE EEVFDAVVVC NGHYTEPRIA
     EIPGIDLWPG KQMHSHNYRT PEQFRDLVVV LIGSAASAVD VSRDIAKVAR EVHVASRSYE
     YDTLGMQSGH DNMWLHPMIE KAHEDGKVTF LDGSYVGADI ILHCTGYKYH FPFLETNGIV
     SVDDNRVGPL YKHVFPPHLA PWLSFVGLPW KAVPFPQFEH QSKWIAGVLS GRISLPSEEE
     MMEDVKDLYS ELKALGIPKR YTHNLANSQF EYNDWLAVQS GSQPSEEWRK EMFLESTRKM
     QARPEVYRDE EIDETLISQA HEDFAKFPSH R
//
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