GSOX2_ARATH
ID GSOX2_ARATH Reviewed; 457 AA.
AC Q94K43; Q9SXE3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Flavin-containing monooxygenase FMO GS-OX2;
DE EC=1.14.13.237 {ECO:0000269|PubMed:18799661};
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase 2;
GN Name=FMOGS-OX2; OrderedLocusNames=At1g62540; ORFNames=T3P18.10;
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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
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.
CC {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 -!- DISRUPTION PHENOTYPE: Increased accumulation of methylthiobutyl,
CC -pentyl, -heptyl and -octyl glucosinolates in leaves and seeds.
CC {ECO:0000269|PubMed:18799661}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43611.1; Type=Erroneous gene model prediction; Evidence={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; AC005698; AAD43611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33977.1; -; Genomic_DNA.
DR EMBL; AF370313; AAK44128.1; -; mRNA.
DR EMBL; AY063099; AAL34273.1; -; mRNA.
DR RefSeq; NP_001320894.1; NM_001334036.1.
DR RefSeq; NP_564796.1; NM_104933.3.
DR AlphaFoldDB; Q94K43; -.
DR SMR; Q94K43; -.
DR STRING; 3702.AT1G62540.1; -.
DR PaxDb; Q94K43; -.
DR PRIDE; Q94K43; -.
DR EnsemblPlants; AT1G62540.1; AT1G62540.1; AT1G62540.
DR GeneID; 842551; -.
DR Gramene; AT1G62540.1; AT1G62540.1; AT1G62540.
DR KEGG; ath:AT1G62540; -.
DR Araport; AT1G62540; -.
DR TAIR; locus:2203871; AT1G62540.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; Q94K43; -.
DR OMA; QPVEPWR; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q94K43; -.
DR BioCyc; MetaCyc:AT1G62540-MON; -.
DR BRENDA; 1.14.13.237; 399.
DR PRO; PR:Q94K43; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94K43; baseline and differential.
DR Genevisible; Q94K43; 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: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; -; 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 PIRSF; PIRSF000332; FMO; 1.
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..457
FT /note="Flavin-containing monooxygenase FMO GS-OX2"
FT /id="PRO_0000360992"
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 457 AA; 52103 MW; 1E53BEFCBC91F080 CRC64;
MAPAQNPISS QHVVVIGAGA AGLVAARELS REGHTVVVLE REKEVGGLWI YSPKAESDPL
SLDPTRSIVH SSVYESLRTN LPRECMGFTD FPFVPRFDDE SRDSRRYPSH MEVLAYLQDF
AREFNLEEMV RFEIEVVRVE PVNGKWRVWS KTSGGVSHDE IFDAVVVCSG HYTEPNVAHI
PGIKSWPGKQ IHSHNYRVPG PFENEVVVVI GNFASGADIS RDIAKVAKEV HIASRASEFD
TYEKLPVPRN NLWIHSEIDT AYEDGSIVFK NGKVVYADSI VYCTGYKYRF TFLETNGYMN
IDENRVEHLY KHVFPPALSP GLSFVGLPSM GIQFVMFEIQ SKWVAAVLSR RVTLPTEDKM
MEDISAWYAS LDAVGIPKRY THKLGKIQSE YLNWVAEECG CPLVEHWRNQ QIVRGYQRLV
SHPETYRDEW DDNDLMEEAY EDFARKKLIS FHPSHIL
