GSOX1_ARATH
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 03-AUG-2022, entry version 138.
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 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 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 + 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: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; 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 STRING; 3702.AT1G65860.1; -.
DR PaxDb; Q9SS04; -.
DR PRIDE; Q9SS04; -.
DR ProteomicsDB; 248515; -.
DR EnsemblPlants; AT1G65860.1; AT1G65860.1; AT1G65860.
DR GeneID; 842897; -.
DR Gramene; AT1G65860.1; AT1G65860.1; AT1G65860.
DR KEGG; ath:AT1G65860; -.
DR Araport; AT1G65860; -.
DR TAIR; locus:2009754; AT1G65860.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; Q9SS04; -.
DR OMA; YFSHHVP; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q9SS04; -.
DR BioCyc; MetaCyc:AT1G65860-MON; -.
DR BRENDA; 1.14.13.237; 399.
DR PRO; PR:Q9SS04; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SS04; baseline and differential.
DR Genevisible; Q9SS04; AT.
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 Gene3D; 3.50.50.60; -; 2.
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 PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; SSF51905; 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
