GSOX5_ARATH
ID GSOX5_ARATH Reviewed; 459 AA.
AC A8MRX0; Q9FWW4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Flavin-containing monooxygenase FMO GS-OX5;
DE EC=1.14.13.237 {ECO:0000269|PubMed:18799661};
DE AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase 5;
GN Name=FMOGS-OX5; OrderedLocusNames=At1g12140; ORFNames=T28K15.12;
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] (ISOFORM 1).
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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
CC into methylsulfinylalkyl glucosinolates. Specific for 8-methylthiooctyl
CC (8-MTO) glucosinolates. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8MRX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MRX0-2; Sequence=VSP_036206;
CC -!- DISRUPTION PHENOTYPE: Increased accumulation of methylthiooctyl
CC glucosinolates in seeds. {ECO:0000269|PubMed:18799661}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AC022522; AAG12579.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28841.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28842.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60976.1; -; Genomic_DNA.
DR EMBL; BT030387; ABO45690.1; -; mRNA.
DR PIR; D86256; D86256.
DR RefSeq; NP_001077522.1; NM_001084053.1. [A8MRX0-2]
DR RefSeq; NP_001323223.1; NM_001332018.1. [A8MRX0-1]
DR RefSeq; NP_172678.3; NM_101086.5. [A8MRX0-1]
DR AlphaFoldDB; A8MRX0; -.
DR SMR; A8MRX0; -.
DR STRING; 3702.AT1G12140.1; -.
DR PaxDb; A8MRX0; -.
DR PRIDE; A8MRX0; -.
DR ProteomicsDB; 247298; -. [A8MRX0-1]
DR EnsemblPlants; AT1G12140.1; AT1G12140.1; AT1G12140. [A8MRX0-1]
DR EnsemblPlants; AT1G12140.2; AT1G12140.2; AT1G12140. [A8MRX0-2]
DR EnsemblPlants; AT1G12140.3; AT1G12140.3; AT1G12140. [A8MRX0-1]
DR GeneID; 837766; -.
DR Gramene; AT1G12140.1; AT1G12140.1; AT1G12140. [A8MRX0-1]
DR Gramene; AT1G12140.2; AT1G12140.2; AT1G12140. [A8MRX0-2]
DR Gramene; AT1G12140.3; AT1G12140.3; AT1G12140. [A8MRX0-1]
DR KEGG; ath:AT1G12140; -.
DR Araport; AT1G12140; -.
DR TAIR; locus:2201971; AT1G12140.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_3_0_1; -.
DR InParanoid; A8MRX0; -.
DR OMA; PSYPFWN; -.
DR PhylomeDB; A8MRX0; -.
DR BioCyc; MetaCyc:AT1G12140-MON; -.
DR BRENDA; 1.14.13.237; 399.
DR PRO; PR:A8MRX0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A8MRX0; baseline and differential.
DR Genevisible; A8MRX0; AT.
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:0004497; F:monooxygenase activity; IDA:TAIR.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IDA:TAIR.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0048444; P:floral organ morphogenesis; IGI:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0046885; P:regulation of hormone biosynthetic process; IMP:TAIR.
DR GO; GO:0046620; P:regulation of organ growth; 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 Alternative splicing; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..459
FT /note="Flavin-containing monooxygenase FMO GS-OX5"
FT /id="PRO_0000360995"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 212..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT VAR_SEQ 183..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036206"
SQ SEQUENCE 459 AA; 52104 MW; 60BA3FE961B9A40D CRC64;
MAPARTRVNS LNVAVIGAGA AGLVAARELR RENHTVVVFE RDSKVGGLWV YTPNSEPDPL
SLDPNRTIVH SSVYDSLRTN LPRECMGYRD FPFVPRPEDD ESRDSRRYPS HREVLAYLED
FAREFKLVEM VRFKTEVVLV EPEDKKWRVQ SKNSDGISKD EIFDAVVVCN GHYTEPRVAH
VPGIDSWPGK QIHSHNYRVP DQFKDQVVVV IGNFASGADI SRDITGVAKE VHIASRSNPS
KTYSKLPGSN NLWLHSMIES VHEDGTIVFQ NGKVVQADTI VHCTGYKYHF PFLNTNGYIT
VEDNCVGPLY EHVFPPALAP GLSFIGLPWM TLQFFMFELQ SKWVAAALSG RVTLPSEEKM
MEDVTAYYAK REAFGQPKRY THRLGGGQVD YLNWIAEQIG APPGEQWRYQ EINGGYYRLA
TQSDTFRDKW DDDHLIVEAY EDFLRQKLIS SLPSQLLES
