GSXL9_ARATH
ID GSXL9_ARATH Reviewed; 460 AA.
AC Q9FF12;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Flavin-containing monooxygenase FMO GS-OX-like 9;
DE EC=1.8.-.-;
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase-like 9;
GN OrderedLocusNames=At5g07800; ORFNames=MXM12.4;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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).
CC -!- FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of
CC any chain length into methylsulfinylalkyl glucosinolates.
CC {ECO:0000250}.
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=BT002806; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB005249; BAB09944.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91206.1; -; Genomic_DNA.
DR EMBL; BT002806; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_196397.1; NM_120862.4.
DR AlphaFoldDB; Q9FF12; -.
DR SMR; Q9FF12; -.
DR STRING; 3702.AT5G07800.1; -.
DR PaxDb; Q9FF12; -.
DR PRIDE; Q9FF12; -.
DR ProteomicsDB; 247230; -.
DR EnsemblPlants; AT5G07800.1; AT5G07800.1; AT5G07800.
DR GeneID; 830673; -.
DR Gramene; AT5G07800.1; AT5G07800.1; AT5G07800.
DR KEGG; ath:AT5G07800; -.
DR Araport; AT5G07800; -.
DR TAIR; locus:2177813; AT5G07800.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_3_1; -.
DR InParanoid; Q9FF12; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q9FF12; -.
DR BioCyc; ARA:AT5G07800-MON; -.
DR PRO; PR:Q9FF12; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF12; baseline and differential.
DR Genevisible; Q9FF12; 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; -; 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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..460
FT /note="Flavin-containing monooxygenase FMO GS-OX-like 9"
FT /id="PRO_0000401964"
FT BINDING 20..25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 222..227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 52337 MW; 6E1A2411ED1AAE7B CRC64;
MVTFTSEASR SRSKKVCVIG AGPAGLVSAR ELRKEGHKVV VLEQNEDVGG QWFYQPNVEE
EDPLGRSSGS INGELKVHSS IYSSLRLTSP REIMGYSDFP FLAKKGRDMR RFPGHKELWL
YLKDFSEAFG LREMIRFNVR VEFVGEKEEE DDVKKWIVRS REKFSGKVME EIFDAVVVAT
GHYSHPRLPS IKGMDSWKRK QIHSHVYRVP DPFRNEVVVV VGNSMSGQDI SMELVEVAKE
VHLSAKTLDI SSGLSKVISK HPNLLIHPQI ESLEDDGKVI FVDGSWVVAD TILYCTGYSY
KFPFLESKGR IEVDDDRVGP LFEHTFPPCL SPSLSFVGIP RKLIGFPFFE AQAKWIAQVL
SGKSSLPSPD QMLQSVDEFY RSRDLAGVPK HNTHDIADFT YCDKYADYVG FPHLEDWRKL
LCLSALNNSQ ENLETYRDSW DDHELLQEAL QSSHFTNFNS
