ID   G2OX_PHACN              Reviewed;         332 AA.
AC   Q9XG83;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase;
DE            EC=1.14.11.13;
DE   AltName: Full=GA 2-oxidase;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase;
DE   AltName: Full=Gibberellin 2-oxidase;
GN   Name=GA2OX1;
OS   Phaseolus coccineus (Scarlet runner bean) (Phaseolus multiflorus).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3886;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=10200325; DOI=10.1073/pnas.96.8.4698;
RA   Thomas S.G., Phillips A.L., Hedden P.;
RT   "Molecular cloning and functional expression of gibberellin 2-oxidases,
RT   multifunctional enzymes involved in gibberellin deactivation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4698-4703(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:10200325}.
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA2OX subfamily. {ECO:0000305}.
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DR   EMBL; AJ132438; CAB41036.1; -; mRNA.
DR   AlphaFoldDB; Q9XG83; -.
DR   SMR; Q9XG83; -.
DR   BioCyc; MetaCyc:MON-11631; -.
DR   BRENDA; 1.14.11.13; 4739.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0052634; F:C-19 gibberellin 2-beta-dioxygenase activity; IEA:UniProtKB-EC.
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..332
FT                   /note="Gibberellin 2-beta-dioxygenase"
FT                   /id="PRO_0000067310"
FT   DOMAIN          175..280
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255"
FT   BINDING         204
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         206
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         261
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   332 AA;  37150 MW;  00CDEBFD2C23D8A5 CRC64;
     MVVLSQPALN QFFLLKPFKS TPLFTGIPVV DLTHPDAKNL IVNACRDFGF FKLVNHGVPL
     ELMANLENEA LRFFKKSQSE KDRAGPPDPF GYGSKRIGPN GDVGWVEYLL LNTNPDVISP
     KSLCIFRENP HHFRAVVENY ITAVKNMCYA VLELMAEGLG IRQRNTLSRL LKDEKSDSCF
     RLNHYPPCPE VQALNRNLVG FGEHTDPQII SVLRSNSTSG LQICLTDGTW VSVPPDQTSF
     FINVGDALQV MTNGRFKSVK HRVLADTTKS RLSMIYFGGP ALSENIAPLP SVMLKGEECL
     YKEFTWCEYK KAAYTSRLAD NRLAPFQKSA AD