ID   GSOX1_ARATH             Reviewed;         459 AA.
AC   Q9SS04;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=Flavin-containing monooxygenase FMO GS-OX1;
DE            EC=1.14.13.237 {ECO:0000269|PubMed:17461789};
DE   AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase 1;
DE   AltName: Full=Putative flavin-containing monooxygenase 3;
GN   Name=FMOGS-OX1; Synonyms=FMO3; OrderedLocusNames=At1g65860;
GN   ORFNames=F12P19.2;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
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   -!- FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates
CC       into methylsulfinylalkyl glucosinolates. Able to S-oxygenate both
CC       desulfo- and intact 4-methylthiobutyl glucosinolates, but no activity
CC       with methionine, dihomomethionine or 5-methylthiopentaldoxime.
CC       {ECO:0000269|PubMed:17461789}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-
CC         glucoside + NADPH + O2 + H(+) = a (Z)-omega-(methylsulfinyl)-alkyl-
CC         glucosinolate + NADP(+) + H2O; Xref=Rhea:RHEA:42208, Rhea:RHEA-
CC         COMP:13194, Rhea:RHEA-COMP:13195, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:136434, ChEBI:CHEBI:136435;
CC         EC=1.14.13.237; Evidence={ECO:0000269|PubMed:17461789};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Mainly expressed in leaves. Low levels in flowers
CC       and seeds. {ECO:0000269|PubMed:17461789}.
CC   -!- DISRUPTION PHENOTYPE: Increased accumulation of methylthiobutyl,
CC       -pentyl and -heptyl glucosinolates in leaves. No effects in seeds.
CC       {ECO:0000269|PubMed:17461789}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC009513; AAF06046.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34434.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7032224.1; -; Genomic_DNA.
DR   EMBL; BT000473; AAN17450.1; -; mRNA.
DR   EMBL; BT002190; AAN72201.1; -; mRNA.
DR   PIR; F96682; F96682.
DR   RefSeq; NP_176761.1; NM_105258.3.
DR   AlphaFoldDB; Q9SS04; -.
DR   SMR; Q9SS04; -.
DR   FunCoup; Q9SS04; 514.
DR   STRING; 3702.Q9SS04; -.
DR   PaxDb; 3702-Q9SS04; -.
DR   ProteomicsDB; 248515; -.
DR   GeneID; 842897; -.
DR   KEGG; ath:AT1G65860; -.
DR   Araport; AT1G65860; -.
DR   TAIR; AT1G65860; FMO GS-OX1.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_3_0_1; -.
DR   InParanoid; Q9SS04; -.
DR   OMA; EENIGKW; -.
DR   OrthoDB; 66881at2759; -.
DR   PhylomeDB; Q9SS04; -.
DR   BioCyc; MetaCyc:AT1G65860-MONOMER; -.
DR   BRENDA; 1.14.13.237; 399.
DR   PRO; PR:Q9SS04; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SS04; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0080102; F:3-methylthiopropyl glucosinolate S-oxygenase activity; IMP:TAIR.
DR   GO; GO:0080103; F:4-methylthiopropyl glucosinolate S-oxygenase activity; IDA:TAIR.
DR   GO; GO:0080104; F:5-methylthiopropyl glucosinolate S-oxygenase activity; IMP:TAIR.
DR   GO; GO:0080105; F:6-methylthiopropyl glucosinolate S-oxygenase activity; IMP:TAIR.
DR   GO; GO:0080106; F:7-methylthiopropyl glucosinolate S-oxygenase activity; IMP:TAIR.
DR   GO; GO:0080107; F:8-methylthiopropyl glucosinolate S-oxygenase activity; IDA:TAIR.
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   GO; GO:0033506; P:glucosinolate biosynthetic process from homomethionine; IMP:TAIR.
DR   FunFam; 3.50.50.60:FF:000099; Flavin-containing monooxygenase; 1.
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   InterPro; IPR050346; FMO-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..459
FT                   /note="Flavin-containing monooxygenase FMO GS-OX1"
FT                   /id="PRO_0000360991"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         211..216
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   459 AA;  52309 MW;  D5115E9CDEA57E0C CRC64;
     MAPTQNTICS KHVAVIGAGA AGLVTARELR REGHTVVVFD REKQVGGLWN YSSKADSDPL
     SLDTTRTIVH TSIYESLRTN LPRECMGFTD FPFVPRIHDI SRDSRRYPSH REVLAYLQDF
     AREFKIEEMV RFETEVVCVE PVNGKWSVRS KNSVGFAAHE IFDAVVVCSG HFTEPNVAHI
     PGIKSWPGKQ IHSHNYRVPG PFNNEVVVVI GNYASGADIS RDIAKVAKEV HIASRASESD
     TYQKLPVPQN NLWVHSEIDF AHQDGSILFK NGKVVYADTI VHCTGYKYYF PFLETNGYIN
     INENRVEPLY KHVFLPALAP SLSFIGLPGM AIQFVMFEIQ SKWVAAVLSG RVILPSQDKM
     MEDIIEWYAT LDVLGIPKRH THKLGKISCE YLNWIAEECH CSPVENWRIQ EVERGFQRMV
     SHPEIYRDEW DDDDLMEEAY KDFARKKLIS SHPSYFLES
//