ID   FMO2_ARATH              Reviewed;         459 AA.
AC   Q9FKE7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Putative flavin-containing monooxygenase 2;
DE            EC=1.14.13.-;
GN   Name=FMO2; OrderedLocusNames=At5g45180; ORFNames=K18C1.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA   Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT   "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT   aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL   Plant J. 50:902-910(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11391.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB012240; BAB11391.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002688; AED95213.1; -; Genomic_DNA.
DR   RefSeq; NP_199331.2; NM_123886.2.
DR   AlphaFoldDB; Q9FKE7; -.
DR   SMR; Q9FKE7; -.
DR   STRING; 3702.AT5G45180.1; -.
DR   PaxDb; Q9FKE7; -.
DR   PRIDE; Q9FKE7; -.
DR   EnsemblPlants; AT5G45180.1; AT5G45180.1; AT5G45180.
DR   GeneID; 834554; -.
DR   Gramene; AT5G45180.1; AT5G45180.1; AT5G45180.
DR   KEGG; ath:AT5G45180; -.
DR   Araport; AT5G45180; -.
DR   TAIR; locus:2153353; AT5G45180.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_9_3_1; -.
DR   InParanoid; Q9FKE7; -.
DR   OMA; HAFEEDY; -.
DR   OrthoDB; 405736at2759; -.
DR   BioCyc; ARA:AT5G45180-MON; -.
DR   PRO; PR:Q9FKE7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKE7; differential.
DR   Genevisible; Q9FKE7; AT.
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; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..459
FT                   /note="Putative flavin-containing monooxygenase 2"
FT                   /id="PRO_0000249422"
FT   BINDING         17..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         46..47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         217..220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
SQ   SEQUENCE   459 AA;  52318 MW;  BEE856179CDA4BF2 CRC64;
     MAYNYNMHTS SRVAIIGAGV SGLAAAKHLA RHHPQVFEAS DSIGGVWRKC TYETTKLQSV
     RVSYELSDFL WPNRGESSFP TYVDVLDYLE AYAKHFNLVK FIKFNSKVVE LRFIGDGKTL
     QMGDLGAYGN LLPGKPVWEV AVNTGDGDIQ WHAFEYVVVC AGKYGDVPRT PTFPVKKGPE
     IFKGKVLHSM DYSKLQKEKA SQLLHGKKVA VIGFKKSAID LALESALANQ GKEGKTCTMV
     VRTPHWVIPH YWRATVSKFI ESYVLWKLPL EKYGLKPDHA FEEDYASCQM ALVPEKFFEE
     ADKGMIRFKR TTNWWFYDEG IEFEDGTTLE ADVVILATGY DGMKKLKAIV PEPFRSWLEF
     PWGIMPLYRG TIHPLIPNMG FIGYVQSSSN LKSSELHSRW LSQLLDGKFT LPSKEKMLDQ
     FLKEMHVMRR SSRFFKNHCF STFSIQHADD LSKDMNLKP