ID   AOP1V_ARATH             Reviewed;         301 AA.
AC   Q944Z5;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable 2-oxoglutarate-dependent dioxygenase AOP1;
DE            EC=1.14.11.-;
DE   Flags: Fragment;
GN   Name=AOP1;
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 GENE FAMILY.
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: Probable 2-oxoglutarate-dependent dioxygenase that may be
CC       involved in glucosinolates biosynthesis. May play a role in the
CC       production of aliphatic glucosinolates (By similarity). {ECO:0000250}.
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; AF418247; AAL14682.1; -; mRNA.
DR   AlphaFoldDB; Q944Z5; -.
DR   SMR; Q944Z5; -.
DR   ExpressionAtlas; Q944Z5; 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; -; 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   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           <1..>301
FT                   /note="Probable 2-oxoglutarate-dependent dioxygenase AOP1"
FT                   /id="PRO_0000423932"
FT   DOMAIN          158..262
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         188
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         243
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         253
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   NON_TER         1
FT   NON_TER         301
SQ   SEQUENCE   301 AA;  34691 MW;  35FC5F29D566CF81 CRC64;
     PSVSFQLPVI DFSDQNLKPG SSKWDEVTAD VLKALEDYGC FEASFDKLSV ELNRSVFEAM
     EDLFELPIPT KQRNVSSKLF HGYLCHNLYE SLGINDANVL EKVNDFTQQL WPDHGNKSIS
     ETIHLFSEQL VELDLMVRRM IMESFGIEKY IDEHLNSTYY LTRLMKYTSP PDDDDDEETK
     LGLRSHTDKN IITILHQYQV DGLEVKTKDD KWIKVKPSQD SVLVMVGDSL CALLNGRLHS
     PYHRVIMTGK KTRYSTGLFS IPKTGVIIDS PEELVDKEHP RIFKPFEYTD FLHFFQTEAG
     R