GSL_ARATH
ID GSL_ARATH Reviewed; 359 AA.
AC Q9SKK4; Q56WB2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable 2-oxoacid dependent dioxygenase {ECO:0000305};
DE EC=1.14.-.- {ECO:0000269|PubMed:18945935};
GN Name=GSL-OH {ECO:0000303|PubMed:18945935};
GN OrderedLocusNames=At2g25450 {ECO:0000312|Araport:AT2G25450};
GN ORFNames=F13B15.11 {ECO:0000312|EMBL:AAD20704.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, POLYMORPHISM, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Abd-0, cv. Ag-0, cv. Ang-0, cv. Bla-10, cv. Bs-1, cv. Bur-0,
RC cv. Cal-0, cv. Cnt-1, cv. Columbia, cv. Cvi-0, cv. Di-0, cv. Di-1,
RC cv. Edi-0, cv. Ei-2, cv. Ema-1, cv. Et-0, cv. Ge-0, cv. HOG, cv. Kas-1,
RC cv. Kon, cv. Landsberg erecta, cv. Lc-0, cv. Lip-0, cv. Lo-2, cv. Mir-0,
RC cv. Mrk-0, cv. Mt-0, cv. Pog-0, cv. Rd-0, cv. Rou-0, cv. Sf-1, cv. Sha,
RC cv. Sorbo, cv. Tac-0, cv. Tsu-1, cv. Wassilewskija, cv. Wei-0, and
RC cv. Yo-0;
RX PubMed=18945935; DOI=10.1104/pp.108.129981;
RA Hansen B.G., Kerwin R.E., Ober J.A., Lambrix V.M., Mitchell-Olds T.,
RA Gershenzon J., Halkier B.A., Kliebenstein D.J.;
RT "A novel 2-oxoacid-dependent dioxygenase involved in the formation of the
RT goiterogenic 2-hydroxybut-3-enyl glucosinolate and generalist insect
RT resistance in Arabidopsis.";
RL Plant Physiol. 148:2096-2108(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-359.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for the hydroxylation of but-3-enyl glucosinolate
CC to 2-hydroxybut-3-enyl glucosinolate, which is toxic to insects,
CC bacteria and nematodes, inhibits seed germination and produces bitter
CC flavors. {ECO:0000269|PubMed:18945935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + gluconapin + O2 = A + H2O + progoitrin;
CC Xref=Rhea:RHEA:60628, ChEBI:CHEBI:5411, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:183096; Evidence={ECO:0000269|PubMed:18945935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60629;
CC Evidence={ECO:0000269|PubMed:18945935};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- TISSUE SPECIFICITY: Expressed in leaves and seeds. All cultivars with
CC seed-only-functional allele have low to non-detectable GSL-OH
CC expression in the leaves. {ECO:0000269|PubMed:18945935}.
CC -!- POLYMORPHISM: Cv. Adb-0, cv. Ag-0, cv. Ang-0, cv. Bla-10, cv. Bs-1, cv.
CC Bur-0, cv. Cal-0, cv. Cnt-1, cv. Columbia, cv. Di-1, cv. Edi-0, cv. Ei-
CC 2, cv. Ema-1, cv. Et-0, cv. Ge-0, cv. Lc-0, cv. Lo-2, cv. Mir-0, cv.
CC Mrk-0, cv. Mt-0, cv. Pog-0, cv. Rd-0, cv. Rou-0, cv. Sf-1, cv. Tac-0,
CC cv. Wei-0 and cv. Yo-0 contain a leaf- and seed-functional allele. Cv.
CC Di-0, cv. Kas-1, cv. Lip-0, cv. Landsberg erecta, cv. Sha, cv. Sorbo,
CC cv. Tsu-1 and cv. Wassilewskija contain a seed-only-functional allele.
CC Cv. Cvi-0, cv. Hodja-Obi-Garm and cv. Kon contain a null allele. The
CC null allele in cv. Cvi-0 is produced by 5 amino acid substitutions
CC while the one in cv. Kon or cv. Hodja-Obi-Garm is produced by a
CC substitution generating a stop codon at position 132.
CC {ECO:0000269|PubMed:18945935}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit a complete absence of 2-
CC hydroxybut-3-enyl glucosinolate accumulation and a decreased resistance
CC to generalist herbivory. {ECO:0000269|PubMed:18945935}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95147.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006300; AAD20704.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07703.1; -; Genomic_DNA.
DR EMBL; AY050787; AAK92722.1; -; mRNA.
DR EMBL; AY114055; AAM45103.1; -; mRNA.
DR EMBL; AK222132; BAD95147.1; ALT_INIT; mRNA.
DR PIR; E84648; E84648.
DR RefSeq; NP_180115.1; NM_128102.6.
DR AlphaFoldDB; Q9SKK4; -.
DR SMR; Q9SKK4; -.
DR BioGRID; 2435; 1.
DR STRING; 3702.AT2G25450.1; -.
DR iPTMnet; Q9SKK4; -.
DR MetOSite; Q9SKK4; -.
DR PaxDb; Q9SKK4; -.
DR PRIDE; Q9SKK4; -.
DR ProteomicsDB; 248495; -.
DR EnsemblPlants; AT2G25450.1; AT2G25450.1; AT2G25450.
DR GeneID; 817083; -.
DR Gramene; AT2G25450.1; AT2G25450.1; AT2G25450.
DR KEGG; ath:AT2G25450; -.
DR Araport; AT2G25450; -.
DR TAIR; locus:2040045; AT2G25450.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_0_0_1; -.
DR InParanoid; Q9SKK4; -.
DR OMA; IMREYSK; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9SKK4; -.
DR BioCyc; ARA:AT2G25450-MON; -.
DR BioCyc; MetaCyc:AT2G25450-MON; -.
DR PRO; PR:Q9SKK4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKK4; baseline and differential.
DR Genevisible; Q9SKK4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
DR GO; GO:0062131; F:3-butenylglucosinolate 2-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..359
FT /note="Probable 2-oxoacid dependent dioxygenase"
FT /id="PRO_0000357026"
FT DOMAIN 207..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 329..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VARIANT 105
FT /note="G -> S (in strain: cv. Cvi-0)"
FT VARIANT 184
FT /note="L -> F (in strain: cv. Cvi-0)"
FT VARIANT 218
FT /note="P -> H (in strain: cv. Cvi-0)"
FT VARIANT 254
FT /note="G -> E (in strain: cv. Cvi-0)"
FT VARIANT 288
FT /note="R -> I (in strain: cv. Cvi-0)"
SQ SEQUENCE 359 AA; 40351 MW; 14CC7C503796EA96 CRC64;
MAENYDRASE LKAFDEMKIG VKGLVDAGVT KVPRIFHNPH VNVANPKPTS TVVMIPTIDL
GGVFESTVVR ESVVAKVKDA MEKFGFFQAI NHGVPLDVME KMINGIRRFH DQDPEVRKMF
YTRDKTKKLK YHSNADLYES PAASWRDTLS CVMAPDVPKA QDLPEVCGEI MLEYSKEVMK
LAELMFEILS EALGLSPNHL KEMDCAKGLW MLCHCFPPCP EPNRTFGGAQ HTDRSFLTIL
LNDNNGGLQV LYDGYWIDVP PNPEALIFNV GDFLQLISND KFVSMEHRIL ANGGEEPRIS
VACFFVHTFT SPSSRVYGPI KELLSELNPP KYRDTTSESS NHYVARKPNG NSSLDHLRI
