ID   AOP3V_ARATH             Reviewed;         410 AA.
AC   Q944X7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=2-oxoglutarate-dependent dioxygenase AOP3;
DE            EC=1.14.11.-;
GN   Name=AOP3;
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 [MRNA], AND FUNCTION.
RC   STRAIN=cv. Cvi-0;
RX   PubMed=11251105; DOI=10.2307/3871415;
RA   Kliebenstein D.J., Lambrix V.M., Reichelt M., Gershenzon J.,
RA   Mitchell-Olds T.;
RT   "Gene duplication in the diversification of secondary metabolism: tandem 2-
RT   oxoglutarate-dependent dioxygenases control glucosinolate biosynthesis in
RT   Arabidopsis.";
RL   Plant Cell 13:681-693(2001).
CC   -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in
CC       glucosinolates biosynthesis. Catalyzes the conversion of
CC       methylsulfinylalkyl glucosinolates to hydroxyalkyl glucosinolates.
CC       {ECO:0000269|PubMed:11251105}.
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: AOP1, AOP2 and AOP3 are found in tandem and inverted
CC       duplications on chromosome IV and encode 2-oxoglutarate-dependent
CC       dioxygenases involved in glucosinolates biosynthesis. In cv. Columbia,
CC       AOP2 (AC Q9ZTA2) cDNA contains a 5-bp deletion that leads to a non-
CC       functional protein and AOP3 (AC Q9ZTA1) is not expressed. The
CC       functional and expressed alleles for AOP2 (AC Q945B5) and AOP3 (AC
CC       Q945B4) are found in cv. Cvi and cv. Landsberg erecta, respectively. No
CC       ecotype coexpresses both AOP2 and AOP3 genes. The catalytic role of
CC       AOP1 is still uncertain (PubMed:11251105).
CC       {ECO:0000305|PubMed:11251105}.
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DR   EMBL; AF418274; AAL14667.1; -; mRNA.
DR   AlphaFoldDB; Q944X7; -.
DR   SMR; Q944X7; -.
DR   HOGENOM; CLU_010119_3_0_1; -.
DR   ExpressionAtlas; Q944X7; baseline and differential.
DR   Genevisible; Q944X7; AT.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 2.
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   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..410
FT                   /note="2-oxoglutarate-dependent dioxygenase AOP3"
FT                   /id="PRO_0000423938"
FT   DOMAIN          258..355
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         278
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         280
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         335
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         346
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   410 AA;  44936 MW;  9B5291DE30FC6639 CRC64;
     MGSCSPQLPL ICLSDQTLKP GSSKWVKVRS DVRKALEDYG CFEAKIDQVS MELQGSVLKA
     MQELFALPTE AKQRNVCPKP FAGYFSHNGL SESFGIKDAN ILEKAHEFTQ QLWPEGNKSI
     KMIQLYAEKL AELDMMVRRL ILESYGIEYF IDEHLNSTYY RMRLMKYIAR PDNDITAAVG
     ANVDNGANDN ADGDANVNDD GASIGVKVNV DVGDDVNDND SVNIGVGVDI NVETNVNGHL
     DAEANGDATA WVVGAVSGNA SVGAKEANVD AELGLPSHTD KSLSGIIYQH QIDGLEVKTK
     EGKWIRVKPA PNTVIFIAGD ALCALMNGRI PSPYHRVRVT EKKKTRYAAA LFSNPKEGYI
     IDSPKELVDE KHPRAFKPFD FVDLFNFYHT EAGRRAPSTL QAFCGVSAGK