GSOX4_ARATH
ID GSOX4_ARATH Reviewed; 461 AA.
AC Q93Y23; Q9SXE0;
DT 20-JAN-2009, 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-OX4;
DE EC=1.14.13.237 {ECO:0000269|PubMed:18799661};
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase 4;
GN Name=FMOGS-OX4; OrderedLocusNames=At1g62570; ORFNames=T3P18.13;
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.
RX PubMed=12481097; DOI=10.1104/pp.008532;
RA Kreps J.A., Wu Y., Chang H.S., Zhu T., Wang X., Harper J.F.;
RT "Transcriptome changes for Arabidopsis in response to salt, osmotic, and
RT cold stress.";
RL Plant Physiol. 130:2129-2141(2002).
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. 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 -!- INDUCTION: Up-regulated in roots by salt, osmotic and cold stresses.
CC {ECO:0000269|PubMed:12481097}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in leaves or seeds; due to
CC the redundancy with other FMO GS-OXs. {ECO:0000269|PubMed:18799661}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005698; AAD43614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33979.1; -; Genomic_DNA.
DR EMBL; AY054642; AAK96833.1; -; mRNA.
DR EMBL; AY081554; AAM10116.1; -; mRNA.
DR PIR; E96651; E96651.
DR RefSeq; NP_564797.1; NM_104935.2.
DR AlphaFoldDB; Q93Y23; -.
DR SMR; Q93Y23; -.
DR STRING; 3702.AT1G62570.1; -.
DR iPTMnet; Q93Y23; -.
DR PaxDb; Q93Y23; -.
DR PRIDE; Q93Y23; -.
DR ProteomicsDB; 247135; -.
DR EnsemblPlants; AT1G62570.1; AT1G62570.1; AT1G62570.
DR GeneID; 842554; -.
DR Gramene; AT1G62570.1; AT1G62570.1; AT1G62570.
DR KEGG; ath:AT1G62570; -.
DR Araport; AT1G62570; -.
DR TAIR; locus:2203901; AT1G62570.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; Q93Y23; -.
DR OMA; PRHTIQT; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q93Y23; -.
DR BioCyc; MetaCyc:AT1G62570-MON; -.
DR BRENDA; 1.14.13.237; 399.
DR PRO; PR:Q93Y23; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Y23; baseline and differential.
DR Genevisible; Q93Y23; AT.
DR GO; GO:0080103; F:4-methylthiopropyl glucosinolate S-oxygenase activity; IDA: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..461
FT /note="Flavin-containing monooxygenase FMO GS-OX4"
FT /id="PRO_0000360994"
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 461 AA; 52459 MW; 789246227497D4B1 CRC64;
MAPAPSPINS QHVAVIGAGA AGLVAARELR REGHTVVVLD REKQVGGLWV YTPETESDEL
GLDPTRPIVH SSVYKSLRTN LPRECMGYKD FPFVPRGDDP SRDSRRYPSH REVLAYLQDF
ATEFNIEEMI RFETEVLRVE PVNGKWRVQS KTGGGFSNDE IYDAVVMCCG HFAEPNIAQI
PGIESWPGRQ THSHSYRVPD PFKDEVVVVI GNFASGADIS RDISKVAKEV HIASRASKSN
TFEKRPVPNN NLWMHSEIDT AHEDGTIVFK NGKVVHADTI VHCTGYKYYF PFLETNNYMR
VDDNRVEPLY KHIFPPALAP GLSFIGLPAM GLQFYMFEVQ SKWVAAVLSG RVTLPSVDEM
MDDLKLSYET QEALGIPKRY THKLGKSQCE YLDWIADLCG FPHVEHWRDQ EVTRGYQRLG
NQPETFRDEW DDDDLMEEAY EDFARLNLIN FHPSRFLESG R
