ID   G2OX2_PEA               Reviewed;         345 AA.
AC   Q9XHM5;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase 2;
DE            EC=1.14.11.13;
DE   AltName: Full=GA 2-oxidase 2;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase 2;
DE   AltName: Full=Gibberellin 2-oxidase 2;
GN   Name=GA2OX2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Torsdag; TISSUE=Seed;
RX   PubMed=10417727; DOI=10.1046/j.1365-313x.1999.00501.x;
RA   Lester D.R., Ross J.J., Smith J.J., Elliott R.C., Reid J.B.;
RT   "Gibberellin 2-oxidation and the SLN gene of Pisum sativum.";
RL   Plant J. 19:65-73(1999).
CC   -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of several biologically
CC       active gibberellins, leading to the homeostatic regulation of their
CC       endogenous level. Catabolism of gibberellins (GAs) plays a central role
CC       in plant development. Converts GA9/GA20 to GA51/GA29 and GA4/GA1 to
CC       GA34/GA8. {ECO:0000269|PubMed:10417727}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + gibberellin A1 + O2 = CO2 + gibberellin A8 +
CC         succinate; Xref=Rhea:RHEA:15005, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58524, ChEBI:CHEBI:58594; EC=1.14.11.13;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in leaves.
CC       {ECO:0000269|PubMed:10417727}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA2OX subfamily. {ECO:0000305}.
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DR   EMBL; AF100954; AAD45424.1; -; mRNA.
DR   AlphaFoldDB; Q9XHM5; -.
DR   SMR; Q9XHM5; -.
DR   EnsemblPlants; Psat6g160000.1; Psat6g160000.1.cds; Psat6g160000.
DR   Gramene; Psat6g160000.1; Psat6g160000.1.cds; Psat6g160000.
DR   BioCyc; MetaCyc:MON-11640; -.
DR   BRENDA; 1.14.11.13; 4872.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0052634; F:C-19 gibberellin 2-beta-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102111; F:gibberellin A20,2-oxoglutarate:oxygen oxidoreductase activity; IEA:EnsemblPlants.
DR   GO; GO:0102924; F:gibberellin A44,2-oxoglutarate:oxygen oxidoreductase activity; IEA:EnsemblPlants.
DR   GO; GO:0102652; F:gibberellin A9,2-oxoglutarate:oxygen oxidoreductase activity; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..345
FT                   /note="Gibberellin 2-beta-dioxygenase 2"
FT                   /id="PRO_0000067312"
FT   DOMAIN          170..285
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255"
FT   BINDING         209
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   345 AA;  38679 MW;  64F4097DF54A64DD CRC64;
     MVVPSPTSMI RTKKTKAVGI PTIDLSLERS QLSELVVKAC EEYGFFKVVN HSVPKEVISR
     LDEEGIEFFS KNSSEKRQAG TSTPFGYGCK NIGPNGDKGE LEYLLLHSNP ISISERSKTI
     AKDHPIKFSC IVNDYIKAVK DLTCEILELA AEGLWVPDKS SLSKIIKDEH SDSLLRINHY
     PPVKKLGNDN WDPSKIQNSN NNNIGFGEHS DPQILTILRS NNVGGLQIST HHGLWIPVPP
     DPSEFYVMVG DALQVLTNGR FVSVRHRVLT NTTKPRMSMM YFAAPPLNWL ISPLSKMVTA
     HSPCLYRPFT WAQYKQAAYA LRLGDTRLDQ FKVQKQEDSN DSHSL