GSXL4_ARATH
ID GSXL4_ARATH Reviewed; 452 AA.
AC Q94BV5; Q8LFQ9; Q9SXD7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Flavin-containing monooxygenase FMO GS-OX-like 4;
DE EC=1.8.-.-;
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase-like 4;
GN OrderedLocusNames=At1g62600; ORFNames=T3P18.16;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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).
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=AAD43617.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005698; AAD43617.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33982.1; -; Genomic_DNA.
DR EMBL; AY039861; AAK63965.1; -; mRNA.
DR EMBL; BT000506; AAN18075.1; -; mRNA.
DR EMBL; AY084698; AAM61259.1; -; mRNA.
DR RefSeq; NP_176448.1; NM_104938.5.
DR AlphaFoldDB; Q94BV5; -.
DR SMR; Q94BV5; -.
DR STRING; 3702.AT1G62600.1; -.
DR iPTMnet; Q94BV5; -.
DR PaxDb; Q94BV5; -.
DR PRIDE; Q94BV5; -.
DR ProteomicsDB; 247227; -.
DR EnsemblPlants; AT1G62600.1; AT1G62600.1; AT1G62600.
DR GeneID; 842557; -.
DR Gramene; AT1G62600.1; AT1G62600.1; AT1G62600.
DR KEGG; ath:AT1G62600; -.
DR Araport; AT1G62600; -.
DR TAIR; locus:2203921; AT1G62600.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; Q94BV5; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q94BV5; -.
DR BioCyc; ARA:AT1G62600-MON; -.
DR PRO; PR:Q94BV5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94BV5; baseline and differential.
DR Genevisible; Q94BV5; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA: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 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..452
FT /note="Flavin-containing monooxygenase FMO GS-OX-like 4"
FT /id="PRO_0000401959"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 217..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 95..98
FT /note="IRSD -> VRSG (in Ref. 4; AAM61259)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="A -> E (in Ref. 4; AAM61259)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="S -> N (in Ref. 4; AAM61259)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..268
FT /note="SVHE -> CVHK (in Ref. 4; AAM61259)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="T -> A (in Ref. 4; AAM61259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 51312 MW; 0270C58C99754AF6 CRC64;
MAPSLSPIRS HHVAVIGAGA AGLVAARELR REGHSVVVFE RQKQVGGTWI YTDHIEPDPL
SVDPTRSVVH SSVYGSLRTN LPRECMGYRD FPFVIRSDVS ESRDPRRFPS HGEVLAYLQD
FAKEFAIEEM IRFDTAVVKV APAAEEGSGK WRIESTEKEK KVLRDEIYDA VVVCNGHYIE
PRHAEIPGIS SWPGKEMHSH NYRIPEPFRD QVVVLIGNSA SADDISRDIA RVAKEVHVAC
RSNAADTYIE RPGYSNLWMH SMIESVHEDG SVVFQNGKTI SVDVIMHCTG YKYHFPFLET
NGNVTVDDNR VGPLYKDVFS PAFAPWLSFV GIPWKVVPFP MFELQSKWIA GVLSGRIPLP
SKEDMMMEIK TLYSTLDAQG IAKRYTHQMG ISQFEYNSWL ASQCGCSETE EWRKEMYFAT
GVKKRAHPET YRDEWDDHHL VSQAYQDFSL YT
