ID   AOP1L_ARATH             Reviewed;         321 AA.
AC   Q945B6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable 2-oxoglutarate-dependent dioxygenase AOP1.2;
DE            EC=1.14.11.-;
GN   Name=AOP1.2;
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. 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: 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; AF417856; AAL14644.1; -; mRNA.
DR   AlphaFoldDB; Q945B6; -.
DR   SMR; Q945B6; -.
DR   ExpressionAtlas; Q945B6; 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..321
FT                   /note="Probable 2-oxoglutarate-dependent dioxygenase
FT                   AOP1.2"
FT                   /id="PRO_0000423933"
FT   DOMAIN          165..270
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         251
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         261
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   321 AA;  36885 MW;  CCF73BB99476B2DE CRC64;
     MDSDFVPPSV SFQLPVIDFS DQNLKPGSSK WDEVKADVLK ALEDYGCFEA FFDKLSVELN
     RSVFEAMEDL FELPIPTKQR NVSSKPFHGY LCHNLYESLG IDDANVLEKV NDFTQQLWPD
     HGNKSISETI HLFSEQLVEL DLMVRRMIME SFGIENYIDE HLNSTYYLTR LMKYTSPPDD
     DDDDEETKLG LRSHTDKNII TILHQYQVDG LEVKTKDDKW IKVKPSQDSV LVMVGDSLCA
     LLNGRLHSPY HRVIMTGKKT RYSTGLFSIP KTGVIIDSPE ELVDKEHPRI FKPFEYTDFL
     HFFQTEAGRI AQSALHAFAA F