ID   AOP3L_ARATH             Reviewed;         410 AA.
AC   Q945B4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
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. Landsberg erecta;
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       Note=Binds 1 Fe(2+) ion per subunit.;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF417859; AAL14647.1; -; mRNA.
DR   AlphaFoldDB; Q945B4; -.
DR   SMR; Q945B4; -.
DR   HOGENOM; CLU_010119_3_0_1; -.
DR   ExpressionAtlas; Q945B4; baseline and differential.
DR   Genevisible; Q945B4; AT.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:UniProtKB.
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_0000423939"
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;  44943 MW;  36801763AB1EA642 CRC64;
     MGSCSPQLPL ICLSDQTLKP GSSKWVKVRS DVRKALEDYG CFEAKIDQVS MELQGSVLKA
     MQELFALPTE AKQRNVCPKP FAGYFSHNGL SESFGIKDAN ILEKAHEFTQ QLWPEGNKSI
     KMIQLYAEKL AELDMMVRRL ILESYGIEYF IDEHLNSTYY RMRLMKYIAR PDNDITAAVG
     ANVDNGANDN ADGDANVNDD GASIGVKVNV DVGDDVNDND SVNIGVGVDI NVETNVNGDL
     DAEANGDATA WVVGAVSGNA SVGAKEANVD AELGLPSHTD KSLSGIIYQH QIDGLEVKTK
     EGKWIRVKPA PNTVIVIAGD ALCALMNGRI PSPYHRVRVT ERKKTRYAAA LFSYPKEGYI
     IDSPKELVDE KHPRAFKPFD FVDLFNFYHT EAGRRAPSTL QAFCGVSAGK