ID G3OX2_ARATH Reviewed; 347 AA.
AC Q9ZT84; Q9C970;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 2 {ECO:0000303|PubMed:11737781};
DE EC=1.14.11.15;
DE AltName: Full=GA 3-oxidase 2 {ECO:0000303|PubMed:11737781};
DE Short=AtGA3ox2 {ECO:0000303|PubMed:11737781};
DE AltName: Full=Gibberellin 3 beta-hydroxylase 2 {ECO:0000305};
DE AltName: Full=Protein GA4 homolog {ECO:0000303|PubMed:9836749};
GN Name=GA3OX2 {ECO:0000303|PubMed:11737781};
GN Synonyms=GA4H {ECO:0000303|PubMed:9836749};
GN OrderedLocusNames=At1g80340 {ECO:0000312|Araport:AT1G80340};
GN ORFNames=F5I6.9 {ECO:0000312|EMBL:AAG52442.1};
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, CATALYTIC ACTIVITY, INDUCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=9836749; DOI=10.1105/tpc.10.12.2115;
RA Yamaguchi S., Smith M.W., Brown R.G.S., Kamiya Y., Sun T.-P.;
RT "Phytochrome regulation and differential expression of gibberellin 3beta-
RT hydroxylase genes in germinating Arabidopsis seeds.";
RL Plant Cell 10:2115-2126(1998).
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 TISSUE SPECIFICITY.
RX PubMed=11737781; DOI=10.1046/j.1365-313x.2001.01168.x;
RA Yamaguchi S., Kamiya Y., Sun T.-P.;
RT "Distinct cell-specific expression patterns of early and late gibberellin
RT biosynthetic genes during Arabidopsis seed germination.";
RL Plant J. 28:443-453(2001).
RN [5]
RP INDUCTION BY COLD.
RX PubMed=14729916; DOI=10.1105/tpc.018143;
RA Yamauchi Y., Ogawa M., Kuwahara A., Hanada A., Kamiya Y., Yamaguchi S.;
RT "Activation of gibberellin biosynthesis and response pathways by low
RT temperature during imbibition of Arabidopsis thaliana seeds.";
RL Plant Cell 16:367-378(2004).
RN [6]
RP CHARACTERIZATION, AND REGULATION.
RX PubMed=15516508; DOI=10.1104/pp.104.047266;
RA Curaba J., Moritz T., Blervaque R., Parcy F., Raz V., Herzog M., Vachon G.;
RT "AtGA3ox2, a key gene responsible for bioactive gibberellin biosynthesis,
RT is regulated during embryogenesis by LEAFY COTYLEDON2 and FUSCA3 in
RT Arabidopsis.";
RL Plant Physiol. 136:3660-3669(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16460513; DOI=10.1111/j.1365-313x.2005.02642.x;
RA Mitchum M.G., Yamaguchi S., Hanada A., Kuwahara A., Yoshioka Y., Kato T.,
RA Tabata S., Kamiya Y., Sun T.P.;
RT "Distinct and overlapping roles of two gibberellin 3-oxidases in
RT Arabidopsis development.";
RL Plant J. 45:804-818(2006).
RN [8]
RP INDUCTION BY AUXIN AND PACLOBUTRAZOL.
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 TISSUE SPECIFICITY.
RX PubMed=17277098; DOI=10.1104/pp.106.093542;
RA Matsushita A., Furumoto T., Ishida S., Takahashi Y.;
RT "AGF1, an AT-hook protein, is necessary for the negative feedback of
RT AtGA3ox1 encoding GA 3-oxidase.";
RL Plant Physiol. 143:1152-1162(2007).
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: Converts the inactive gibberellin (GA) precursors GA9 and
CC GA20 in the bioactives gibberellins GA4 and GA1 (PubMed:9836749).
CC Involved in the production of bioactive GA for vegetative growth and
CC development (PubMed:16460513). {ECO:0000269|PubMed:16460513,
CC ECO:0000269|PubMed:9836749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A20 + O2 = CO2 + gibberellin A1 +
CC succinate; Xref=Rhea:RHEA:10104, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58524, ChEBI:CHEBI:58526; EC=1.14.11.15;
CC Evidence={ECO:0000269|PubMed:9836749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10105;
CC Evidence={ECO:0000269|PubMed:9836749};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q5W726};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for GA9 {ECO:0000269|PubMed:9836749};
CC KM=13 uM for GA20 {ECO:0000269|PubMed:9836749};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC Q9ZT84; Q9FVU9: CSN5B; NbExp=3; IntAct=EBI-25512974, EBI-697501;
CC Q9ZT84; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-25512974, EBI-15192297;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings but also expressed in
CC roots, leaves, stems, flowers, siliques and seeds. Detected
CC predominantly in the hypocotyl and roots of young seedlings and in the
CC petioles and vasculature of leaves. Not expressed in the shoot apical
CC meristem, but found in the elongation zone, the quiescent center cells
CC and the columella cells of the root tips. Found in the cortex and the
CC endodermis of the embryo axis in germinating seeds.
CC {ECO:0000269|PubMed:11737781, ECO:0000269|PubMed:16460513,
CC ECO:0000269|PubMed:17277098}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds and in very young
CC seedlings. Declines to low levels during later stages of development.
CC {ECO:0000269|PubMed:16460513, ECO:0000269|PubMed:9836749}.
CC -!- INDUCTION: Not under feedback regulation. Regulated by phytochrome.
CC Induced by red light pulse and reaches its maximum level after 12
CC hours. Transcriptionally regulated by LEAFY COTYLEDON2 and FUSCA3. Not
CC regulated by cold treatment or auxin. Up-regulated by paclobutrazol.
CC {ECO:0000269|PubMed:14729916, ECO:0000269|PubMed:16905669,
CC ECO:0000269|PubMed:9836749}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; probably due to redundancy
CC with GA3OX1. Ga3ox1 and ga3ox2 double mutant has a severe defect in
CC seed germination and root growth, and a dwarf phenotype.
CC {ECO:0000269|PubMed:16460513}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
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DR EMBL; AF070937; AAC83647.1; -; mRNA.
DR EMBL; AC018848; AAG52442.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36389.1; -; Genomic_DNA.
DR PIR; A96835; A96835.
DR PIR; T51691; T51691.
DR RefSeq; NP_178150.1; NM_106683.2.
DR AlphaFoldDB; Q9ZT84; -.
DR SMR; Q9ZT84; -.
DR BioGRID; 29592; 2.
DR IntAct; Q9ZT84; 2.
DR STRING; 3702.Q9ZT84; -.
DR PaxDb; 3702-AT1G80340-1; -.
DR EnsemblPlants; AT1G80340.1; AT1G80340.1; AT1G80340.
DR GeneID; 844374; -.
DR Gramene; AT1G80340.1; AT1G80340.1; AT1G80340.
DR KEGG; ath:AT1G80340; -.
DR Araport; AT1G80340; -.
DR TAIR; AT1G80340; GA3OX2.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9ZT84; -.
DR OMA; AGKLMWL; -.
DR OrthoDB; 1057251at2759; -.
DR PhylomeDB; Q9ZT84; -.
DR BioCyc; ARA:AT1G80340-MONOMER; -.
DR BioCyc; MetaCyc:AT1G80340-MONOMER; -.
DR BRENDA; 1.14.11.15; 399.
DR SABIO-RK; Q9ZT84; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9ZT84; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZT84; baseline and differential.
DR Genevisible; Q9ZT84; AT.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; TAS:TAIR.
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 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 PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF263; GIBBERELLIN 3-BETA-DIOXYGENASE 2; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..347
FT /note="Gibberellin 3-beta-dioxygenase 2"
FT /id="PRO_0000067314"
FT DOMAIN 197..301
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 292
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 292
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 204
FT /note="V -> A (in Ref. 1; AAC83647)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="I -> V (in Ref. 1; AAC83647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38782 MW; DC5846E65CD44FAB CRC64;
MSSTLSDVFR SHPIHIPLSN PPDFKSLPDS YTWTPKDDLL FSASASDETL PLIDLSDIHV
ATLVGHACTT WGAFQITNHG VPSRLLDDIE FLTGSLFRLP VQRKLKAARS ENGVSGYGVA
RIASFFNKKM WSEGFTVIGS PLHDFRKLWP SHHLKYCEII EEYEEHMQKL AAKLMWFALG
SLGVEEKDIQ WAGPNSDFQG TQAVIQLNHY PKCPEPDRAM GLAAHTDSTL MTILYQNNTA
GLQVFRDDVG WVTAPPVPGS LVVNVGDLLH ILTNGIFPSV LHRARVNHVR SRFSMAYLWG
PPSDIMISPL PKLVDPLQSP LYPSLTWKQY LATKATHFNQ SLSIIRN
//
