ID   AOP2L_ARATH             Reviewed;         432 AA.
AC   Q944Z9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=2-oxoglutarate-dependent dioxygenase AOP2;
DE            EC=1.14.11.-;
GN   Name=AOP2;
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 alkenyl 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; AF418240; AAL14665.1; -; mRNA.
DR   AlphaFoldDB; Q944Z9; -.
DR   SMR; Q944Z9; -.
DR   ExpressionAtlas; Q944Z9; baseline and differential.
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..432
FT                   /note="2-oxoglutarate-dependent dioxygenase AOP2"
FT                   /id="PRO_0000423936"
FT   DOMAIN          281..378
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         303
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         358
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         369
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   432 AA;  47885 MW;  A988945AED52101A CRC64;
     MGSCSLQLPL INLADKTLEP GSSKWAEVRS DVRKALQDFG CFEASYDKVS LELQESIMKT
     MEELFALPVE TKQRNVCPKP YVGYLNHNNL SESLGISNAN ILENINEFTQ QLWPHGDGNE
     NISKTIQLFA EKLVEIDVMV RRMVMESFGI EKYIDDHLKS TEYRMRLMKY IAPPEGDANT
     TVDDYADLLA KLNIDGVEPN VGVKVNADIS DDVNANPSVN AGVGANVNAD TGVNDNLNVD
     AEANGDANIA VGGGVNANTD LGVGVNVNSN VAVNAKTGAT SGDDVEANDD NEEKKLGLPC
     HTDKNLFTVL FQHEIEGLEV KTKDEKWIRV KPSPNTFIVI AGDSLCALMN GRIRAPYHRV
     RVTEKKRTRY TAAIFTCPKP DYVIEAPKEL VDEKHPRLFR PFDYRDLFTF YHSEAGRKIQ
     YTLQAYCAVS EA