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Probable 2-oxoacid dependent dioxygenase (EC 1.14.-.-)

 GSL_ARATH               Reviewed;         359 AA.
Q9SKK4; Q56WB2;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 105.
RecName: Full=Probable 2-oxoacid dependent dioxygenase;
EC=1.14.-.-;
Name=GSL-OH; OrderedLocusNames=At2g25450; ORFNames=F13B15.11;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
POLYMORPHISM, AND TISSUE SPECIFICITY.
STRAIN=cv. Abd-0, cv. Ag-0, cv. Ang-0, cv. Bla-10, cv. Bs-1,
cv. Bur-0, cv. Cal-0, cv. Cnt-1, cv. Columbia, cv. Cvi-0, cv. Di-0,
cv. Di-1, cv. Edi-0, cv. Ei-2, cv. Ema-1, cv. Et-0, cv. Ge-0, cv. HOG,
cv. Kas-1, cv. Kon, cv. Landsberg erecta, cv. Lc-0, cv. Lip-0,
cv. Lo-2, cv. Mir-0, cv. Mrk-0, cv. Mt-0, cv. Pog-0, cv. Rd-0,
cv. Rou-0, cv. Sf-1, cv. Sha, cv. Sorbo, cv. Tac-0, cv. Tsu-1,
cv. Wassilewskija, cv. Wei-0, and cv. Yo-0;
PubMed=18945935; DOI=10.1104/pp.108.129981;
Hansen B.G., Kerwin R.E., Ober J.A., Lambrix V.M., Mitchell-Olds T.,
Gershenzon J., Halkier B.A., Kliebenstein D.J.;
"A novel 2-oxoacid-dependent dioxygenase involved in the formation of
the goiterogenic 2-hydroxybut-3-enyl glucosinolate and generalist
insect resistance in Arabidopsis.";
Plant Physiol. 148:2096-2108(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-359.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Necessary for the hydroxylation of but-3-enyl
glucosinolate to 2-hydroxybut-3-enyl glucosinolate, which is toxic
to insects, bacteria and nematodes, inhibits seed germination and
produces bitter flavors. {ECO:0000269|PubMed:18945935}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- TISSUE SPECIFICITY: Expressed in leaves and seeds. All cultivars
with seed-only-functional allele have low to non-detectable GSL-OH
expression in the leaves. {ECO:0000269|PubMed:18945935}.
-!- POLYMORPHISM: Cv. Adb-0, cv. Ag-0, cv. Ang-0, cv. Bla-10, cv. Bs-
1, cv. Bur-0, cv. Cal-0, cv. Cnt-1, cv. Columbia, cv. Di-1, cv.
Edi-0, cv. Ei-2, cv. Ema-1, cv. Et-0, cv. Ge-0, cv. Lc-0, cv. Lo-
2, cv. Mir-0, cv. Mrk-0, cv. Mt-0, cv. Pog-0, cv. Rd-0, cv. Rou-0,
cv. Sf-1, cv. Tac-0, cv. Wei-0 and cv. Yo-0 contain a leaf-and
seed-functional allele. Cv. Di-0, cv. Kas-1, cv. Lip-0, cv.
Landsberg erecta, cv. Sha, cv. Sorbo, cv. Tsu-1 and cv.
Wassilewskija contain a seed-only-functional allele. Cv. Cvi-0,
cv. Hodja-Obi-Garm and cv. Kon contain a null allele. The null
allele in cv. Cvi-0 is produced by 5 amino acid substitutions
while the one in cv. Kon or cv. Hodja-Obi-Garm is produced by a
substitution generating a stop codon at position 132.
{ECO:0000269|PubMed:18945935}.
-!- DISRUPTION PHENOTYPE: Plants exhibit a complete absence of 2-
hydroxybut-3-enyl glucosinolate accumulation and a decreased
resistance to generalist herbivory. {ECO:0000269|PubMed:18945935}.
-!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD95147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC006300; AAD20704.1; -; Genomic_DNA.
EMBL; CP002685; AEC07703.1; -; Genomic_DNA.
EMBL; AY050787; AAK92722.1; -; mRNA.
EMBL; AY114055; AAM45103.1; -; mRNA.
EMBL; AK222132; BAD95147.1; ALT_INIT; mRNA.
PIR; E84648; E84648.
RefSeq; NP_180115.1; NM_128102.6.
UniGene; At.47589; -.
ProteinModelPortal; Q9SKK4; -.
BioGrid; 2435; 1.
STRING; 3702.AT2G25450.1; -.
iPTMnet; Q9SKK4; -.
PaxDb; Q9SKK4; -.
PRIDE; Q9SKK4; -.
EnsemblPlants; AT2G25450.1; AT2G25450.1; AT2G25450.
GeneID; 817083; -.
Gramene; AT2G25450.1; AT2G25450.1; AT2G25450.
KEGG; ath:AT2G25450; -.
Araport; AT2G25450; -.
TAIR; locus:2040045; AT2G25450.
eggNOG; KOG0143; Eukaryota.
eggNOG; COG3491; LUCA.
HOGENOM; HOG000276735; -.
InParanoid; Q9SKK4; -.
OMA; MATITSD; -.
OrthoDB; EOG09360GGG; -.
PhylomeDB; Q9SKK4; -.
BioCyc; ARA:AT2G25450-MONOMER; -.
BioCyc; MetaCyc:AT2G25450-MONOMER; -.
PRO; PR:Q9SKK4; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SKK4; differential.
Genevisible; Q9SKK4; AT.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:TAIR.
Gene3D; 2.60.120.330; -; 1.
InterPro; IPR026992; DIOX_N.
InterPro; IPR027443; IPNS-like.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
Pfam; PF03171; 2OG-FeII_Oxy; 1.
Pfam; PF14226; DIOX_N; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
2: Evidence at transcript level;
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 359 Probable 2-oxoacid dependent dioxygenase.
/FTId=PRO_0000357026.
DOMAIN 207 308 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 231 231 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 233 233 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 287 287 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
VARIANT 105 105 G -> S (in strain: cv. Cvi-0).
VARIANT 184 184 L -> F (in strain: cv. Cvi-0).
VARIANT 218 218 P -> H (in strain: cv. Cvi-0).
VARIANT 254 254 G -> E (in strain: cv. Cvi-0).
VARIANT 288 288 R -> I (in strain: cv. Cvi-0).
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


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