ID GSOX3_ARATH Reviewed; 462 AA.
AC Q9SXE1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Flavin-containing monooxygenase FMO GS-OX3;
DE EC=1.14.13.237 {ECO:0000269|PubMed:18799661};
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase 3;
GN Name=FMOGS-OX3; OrderedLocusNames=At1g62560; ORFNames=T3P18.12;
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 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 [4]
RP INDUCTION BY AUXIN.
RX PubMed=15047898; DOI=10.1104/pp.103.034736;
RA Goda H., Sawa S., Asami T., Fujioka S., Shimada Y., Yoshida S.;
RT "Comprehensive comparison of auxin-regulated and brassinosteroid-regulated
RT genes in Arabidopsis.";
RL Plant Physiol. 134:1555-1573(2004).
RN [5]
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18799661; DOI=10.1104/pp.108.125757;
RA Li J., Hansen B.G., Ober J.A., Kliebenstein D.J., Halkier B.A.;
RT "Subclade of flavin-monooxygenases involved in aliphatic glucosinolate
RT biosynthesis.";
RL Plant Physiol. 148:1721-1733(2008).
CC -!- FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of
CC any chain length into methylsulfinylalkyl glucosinolates. Prefers
CC probably short-chain methylthioalkyl glucosinolates in cv. Landsberg
CC erecta. {ECO:0000269|PubMed:18799661}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-
CC glucoside + H(+) + NADPH + O2 = a (Z)-omega-(methylsulfinyl)-alkyl-
CC glucosinolate + H2O + NADP(+); 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:18799661};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Down-regulated at late stage by auxin.
CC {ECO:0000269|PubMed:15047898}.
CC -!- DISRUPTION PHENOTYPE: Increased accumulation of methylthiopropyl
CC glucosinolates in leaves and seeds. {ECO:0000269|PubMed:18799661}.
CC -!- MISCELLANEOUS: In contrast to cv. Columbia, cv. Landsberg erecta has
CC predominantly propyl C3 instead of butyl C4 Met-derived glucosinolates.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AC005698; AAD43613.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33978.1; -; Genomic_DNA.
DR EMBL; AF370136; AAK43951.1; -; mRNA.
DR EMBL; AY113858; AAM44906.1; -; mRNA.
DR RefSeq; NP_176444.1; NM_104934.3.
DR AlphaFoldDB; Q9SXE1; -.
DR SMR; Q9SXE1; -.
DR BioGRID; 27774; 1.
DR IntAct; Q9SXE1; 1.
DR STRING; 3702.Q9SXE1; -.
DR iPTMnet; Q9SXE1; -.
DR PaxDb; 3702-AT1G62560-1; -.
DR ProteomicsDB; 247257; -.
DR EnsemblPlants; AT1G62560.1; AT1G62560.1; AT1G62560.
DR GeneID; 842553; -.
DR Gramene; AT1G62560.1; AT1G62560.1; AT1G62560.
DR KEGG; ath:AT1G62560; -.
DR Araport; AT1G62560; -.
DR TAIR; AT1G62560; FMO GS-OX3.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; Q9SXE1; -.
DR OrthoDB; 2453855at2759; -.
DR PhylomeDB; Q9SXE1; -.
DR BioCyc; MetaCyc:AT1G62560-MONOMER; -.
DR BRENDA; 1.14.13.237; 399.
DR PRO; PR:Q9SXE1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXE1; baseline and differential.
DR Genevisible; Q9SXE1; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IDA:TAIR.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
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:SF244; FLAVIN-CONTAINING MONOOXYGENASE FMO GS-OX1-RELATED; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="Flavin-containing monooxygenase FMO GS-OX3"
FT /id="PRO_0000360993"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 212..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 52688 MW; 94FC76E689B93F68 CRC64;
MAPAQNQITS KHVAVIGAGP AGLITSRELR REGHSVVVFE REKQVGGLWV YTPKSDSDPL
SLDPTRSKVH SSIYESLRTN VPRESMGVRD FPFLPRFDDE SRDARRYPNH REVLAYIQDF
AREFKIEEMI RFETEVVRVE PVDNGNWRVQ SKNSGGFLED EIYDAVVVCN GHYTEPNIAH
IPGIKSWPGK QIHSHNYRVP DPFENEVVVV IGNFASGADI SRDIAKVAKE VHIASRAREP
HTYEKISVPQ NNLWMHSEID TTHEDGSIVF KNGKVIFADS IVYCTGYKYN FPFLETNGYL
RIDEKRVEPL YKHVFPPALA PGLAFVGLPA MGIVFVMFEI QSKWVAAVLS GRVTLPSTDK
MMEDINAWYA SLDALGIPKR HTHTIGRIQS EYLNWVAKES GCELVERWRG QEVDGGYLRL
VAHPETYRDE WDDDELIEEA YNDFSRKKLI SVDPSYYLEN GR
//
