G2OX1_ARATH
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 03-AUG-2022, entry version 124.
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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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=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(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 -!- 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; BT002763; AAO22591.1; -; mRNA.
DR EMBL; AY085539; AAM62763.1; -; mRNA.
DR PIR; T52579; T52579.
DR RefSeq; NP_177965.1; NM_106491.2.
DR AlphaFoldDB; Q8LEA2; -.
DR SMR; Q8LEA2; -.
DR BioGRID; 29399; 1.
DR STRING; 3702.AT1G78440.1; -.
DR PaxDb; Q8LEA2; -.
DR PRIDE; Q8LEA2; -.
DR EnsemblPlants; AT1G78440.1; AT1G78440.1; AT1G78440.
DR GeneID; 844180; -.
DR Gramene; AT1G78440.1; AT1G78440.1; AT1G78440.
DR KEGG; ath:AT1G78440; -.
DR Araport; AT1G78440; -.
DR TAIR; locus:2032080; AT1G78440.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q8LEA2; -.
DR OMA; EFCSALN; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q8LEA2; -.
DR BioCyc; ARA:AT1G78440-MON; -.
DR BioCyc; MetaCyc:AT1G78440-MON; -.
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 Genevisible; Q8LEA2; AT.
DR GO; GO:0052634; F:C-19 gibberellin 2-beta-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045487; P:gibberellin catabolic process; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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; 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. 5; AAM62763)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="F -> L (in Ref. 5; AAM62763)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="H -> L (in Ref. 5; AAM62763)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> C (in Ref. 5; 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
