ID   G2OX1_ARATH             Reviewed;         329 AA.
AC   Q8LEA2; Q9XFR8;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase 1;
DE            EC=1.14.11.13;
DE   AltName: Full=GA 2-oxidase 1;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase 1;
DE   AltName: Full=Gibberellin 2-oxidase 1;
GN   Name=GA2OX1; OrderedLocusNames=At1g78440; ORFNames=F3F9.5;
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], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Columbia;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=16139211; DOI=10.1016/j.cub.2005.07.023;
RA   Jasinski S., Piazza P., Craft J., Hay A., Woolley L., Rieu I., Phillips A.,
RA   Hedden P., Tsiantis M.;
RT   "KNOX action in Arabidopsis is mediated by coordinate regulation of
RT   cytokinin and gibberellin activities.";
RL   Curr. Biol. 15:1560-1565(2005).
RN   [8]
RP   INDUCTION BY AUXIN.
RX   PubMed=16905669; DOI=10.1104/pp.106.084871;
RA   Frigerio M., Alabadi D., Perez-Gomez J., Garcia-Carcel L., Phillips A.L.,
RA   Hedden P., Blazquez M.A.;
RT   "Transcriptional regulation of gibberellin metabolism genes by auxin
RT   signaling in Arabidopsis.";
RL   Plant Physiol. 142:553-563(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=18805991; DOI=10.1105/tpc.108.058818;
RA   Rieu I., Eriksson S., Powers S.J., Gong F., Griffiths J., Woolley L.,
RA   Benlloch R., Nilsson O., Thomas S.G., Hedden P., Phillips A.L.;
RT   "Genetic analysis reveals that C19-GA 2-oxidation is a major gibberellin
RT   inactivation pathway in Arabidopsis.";
RL   Plant Cell 20:2420-2436(2008).
RN   [10]
RP   GENE FAMILY.
RX   PubMed=21056641; DOI=10.1016/j.gene.2010.10.010;
RA   Han F., Zhu B.;
RT   "Evolutionary analysis of three gibberellin oxidase genes in rice,
RT   Arabidopsis, and soybean.";
RL   Gene 473:23-35(2011).
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, ECO:0000269|PubMed:18805991}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gibberellin A1 + 2-oxoglutarate + O2 = gibberellin A8 +
CC         succinate + CO2; 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(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in flowers, siliques, and
CC       upper stems. Not expressed in the apex. {ECO:0000269|PubMed:10200325,
CC       ECO:0000269|PubMed:16139211}.
CC   -!- INDUCTION: By gibberellin A3 (GA3). Not regulated by auxin.
CC       {ECO:0000269|PubMed:10200325, ECO:0000269|PubMed:16905669}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA2OX subfamily. {ECO:0000305}.
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DR   EMBL; AJ132435; CAB41007.1; -; mRNA.
DR   EMBL; AC013430; AAF71795.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36106.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7033815.1; -; Genomic_DNA.
DR   EMBL; BT002763; AAO22591.1; -; mRNA.
DR   EMBL; AY085539; AAM62763.1; -; mRNA.
DR   PIR; T52579; T52579.
DR   AlphaFoldDB; Q8LEA2; -.
DR   SMR; Q8LEA2; -.
DR   BioGRID; 29399; 1.
DR   FunCoup; Q8LEA2; 20.
DR   STRING; 3702.Q8LEA2; -.
DR   PaxDb; 3702-Q8LEA2; -.
DR   GeneID; 844180; -.
DR   KEGG; ath:AT1G78440; -.
DR   Araport; AT1G78440; -.
DR   TAIR; AT1G78440; ATGA2OX1.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_3_1; -.
DR   InParanoid; Q8LEA2; -.
DR   OMA; SKANNCK; -.
DR   OrthoDB; 288590at2759; -.
DR   PhylomeDB; Q8LEA2; -.
DR   BioCyc; ARA:AT1G78440-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G78440-MONOMER; -.
DR   BRENDA; 1.14.11.13; 399.
DR   UniPathway; UPA00390; -.
DR   PRO; PR:Q8LEA2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8LEA2; baseline and differential.
DR   GO; GO:0045543; F:gibberellin 2-beta-dioxygenase activity; IDA:TIGR.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045487; P:gibberellin catabolic process; IDA:TIGR.
DR   FunFam; 2.60.120.330:FF:000014; Gibberellin 2-beta-dioxygenase 1; 1.
DR   Gene3D; 2.60.120.330; B-lactam Antibiotic, Isopenicillin N Synthase, Chain; 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_dom.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Gibberellin 2-beta-dioxygenase 1"
FT                   /id="PRO_0000067305"
FT   DOMAIN          165..273
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         199
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         254
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         264
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   CONFLICT        10
FT                   /note="I -> V (in Ref. 6; AAM62763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="F -> L (in Ref. 6; AAM62763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="H -> L (in Ref. 6; AAM62763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="F -> C (in Ref. 6; AAM62763)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  36732 MW;  BBD6B0190C12D37C CRC64;
     MAVLSKPVAI PKSGFSLIPV IDMSDPESKH ALVKACEDFG FFKVINHGVS AELVSVLEHE
     TVDFFSLPKS EKTQVAGYPF GYGNSKIGRN GDVGWVEYLL MNANHDSGSG PLFPSLLKSP
     GTFRNALEEY TTSVRKMTFD VLEKITDGLG IKPRNTLSKL VSDQNTDSIL RLNHYPPCPL
     SNKKTNGGKN VIGFGEHTDP QIISVLRSNN TSGLQINLND GSWISVPPDH TSFFFNVGDS
     LQVMTNGRFK SVRHRVLANC KKSRVSMIYF AGPSLTQRIA PLTCLIDNED ERLYEEFTWS
     EYKNSTYNSR LSDNRLQQFE RKTIKNLLN
//