G2OX2_ARATH
ID G2OX2_ARATH Reviewed; 341 AA.
AC Q9XFR9; F4I385;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
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; OrderedLocusNames=At1g30040; ORFNames=T1P2.6;
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 TISSUE SPECIFICITY, AND INDUCTION BY CYTOKININ.
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 [6]
RP INDUCTION BY AUXIN AND PACLOBUTRAZOL, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
RP 3D-STRUCTURE MODELING, AND 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XFR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XFR9-2; Sequence=VSP_046515, VSP_046516;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in flowers, siliques, and
CC upper stems. Expressed in cotyledons, at the base of the shoot apical
CC meristem and developing leaf primordia. {ECO:0000269|PubMed:10200325,
CC ECO:0000269|PubMed:16139211, ECO:0000269|PubMed:16905669}.
CC -!- INDUCTION: Up-regulated by cytokinin, auxin, paclobutrazol and
CC gibberellin A3 (GA3). {ECO:0000269|PubMed:10200325,
CC ECO:0000269|PubMed:16139211, 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; AJ132436; CAB41008.1; -; mRNA.
DR EMBL; AC022455; AAG52050.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31170.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31171.1; -; Genomic_DNA.
DR EMBL; BT002987; AAO22796.1; -; mRNA.
DR EMBL; BT004464; AAO42458.1; -; mRNA.
DR PIR; T52578; T52578.
DR RefSeq; NP_001031112.1; NM_001036035.2. [Q9XFR9-2]
DR RefSeq; NP_174296.1; NM_102743.3. [Q9XFR9-1]
DR AlphaFoldDB; Q9XFR9; -.
DR SMR; Q9XFR9; -.
DR STRING; 3702.AT1G30040.1; -.
DR PaxDb; Q9XFR9; -.
DR PRIDE; Q9XFR9; -.
DR ProteomicsDB; 230049; -. [Q9XFR9-1]
DR EnsemblPlants; AT1G30040.1; AT1G30040.1; AT1G30040. [Q9XFR9-1]
DR EnsemblPlants; AT1G30040.2; AT1G30040.2; AT1G30040. [Q9XFR9-2]
DR GeneID; 839883; -.
DR Gramene; AT1G30040.1; AT1G30040.1; AT1G30040. [Q9XFR9-1]
DR Gramene; AT1G30040.2; AT1G30040.2; AT1G30040. [Q9XFR9-2]
DR KEGG; ath:AT1G30040; -.
DR Araport; AT1G30040; -.
DR TAIR; locus:2198258; AT1G30040.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9XFR9; -.
DR OMA; CMVLEMI; -.
DR PhylomeDB; Q9XFR9; -.
DR BioCyc; ARA:AT1G30040-MON; -.
DR BioCyc; MetaCyc:AT1G30040-MON; -.
DR BRENDA; 1.14.11.13; 399.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9XFR9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XFR9; baseline and differential.
DR Genevisible; Q9XFR9; 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:0071456; P:cellular response to hypoxia; HEP:TAIR.
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 GO; GO:0010114; P:response to red light; IEP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IEP:TAIR.
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 Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..341
FT /note="Gibberellin 2-beta-dioxygenase 2"
FT /id="PRO_0000067306"
FT DOMAIN 179..283
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 274
FT /evidence="ECO:0000255"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 274
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VAR_SEQ 254..268
FT /note="MTNGRFKSVKHRVLA -> PFPLFFLFFYIYLKI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046515"
FT VAR_SEQ 269..341
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046516"
SQ SEQUENCE 341 AA; 38457 MW; 83125B5324A62F77 CRC64;
MVVLPQPVTL DNHISLIPTY KPVPVLTSHS IPVVNLADPE AKTRIVKACE EFGFFKVVNH
GVRPELMTRL EQEAIGFFGL PQSLKNRAGP PEPYGYGNKR IGPNGDVGWI EYLLLNANPQ
LSSPKTSAVF RQTPQIFRES VEEYMKEIKE VSYKVLEMVA EELGIEPRDT LSKMLRDEKS
DSCLRLNHYP AAEEEAEKMV KVGFGEHTDP QIISVLRSNN TAGLQICVKD GSWVAVPPDH
SSFFINVGDA LQVMTNGRFK SVKHRVLADT RRSRISMIYF GGPPLSQKIA PLPCLVPEQD
DWLYKEFTWS QYKSSAYKSK LGDYRLGLFE KQPLLNHKTL V
