G3OX1_ARATH
ID G3OX1_ARATH Reviewed; 358 AA.
AC Q39103; Q0WTG6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 1;
DE EC=1.14.11.15 {ECO:0000269|PubMed:9625708};
DE AltName: Full=GA 3-oxidase 1;
DE Short=AtGA3ox1;
DE AltName: Full=Gibberellin 3 beta-hydroxylase 1;
GN Name=GA3OX1; Synonyms=GA4 {ECO:0000303|PubMed:9625708};
GN OrderedLocusNames=At1g15550; ORFNames=T16N11.6;
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], MUTAGENESIS OF CYS-220, INDUCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7756830; DOI=10.2307/3869995;
RA Chiang H.-H., Hwang I., Goodman H.M.;
RT "Isolation of the Arabidopsis GA4 locus.";
RL Plant Cell 7:195-201(1995).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9625708; DOI=10.1104/pp.117.2.559;
RA Williams J., Phillips A.L., Gaskin P., Hedden P.;
RT "Function and substrate specificity of the gibberellin 3beta-hydroxylase
RT encoded by the Arabidopsis GA4 gene.";
RL Plant Physiol. 117:559-563(1998).
RN [7]
RP FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9836749; DOI=10.2307/3870788;
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 [8]
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 [9]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15181202; DOI=10.1104/pp.104.041509;
RA Zhou R., Yu M., Pharis R.P.;
RT "16,17-dihydro gibberellin A5 competitively inhibits a recombinant
RT Arabidopsis GA 3beta-hydroxylase encoded by the GA4 gene.";
RL Plant Physiol. 135:1000-1007(2004).
RN [10]
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 [11]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15927942; DOI=10.1093/pcp/pci141;
RA Kim Y.C., Nakajima M., Nakayama A., Yamaguchi I.;
RT "Contribution of gibberellins to the formation of Arabidopsis seed coat
RT through starch degradation.";
RL Plant Cell Physiol. 46:1317-1325(2005).
RN [12]
RP INDUCTION BY LIGHT.
RX PubMed=15923331; DOI=10.1104/pp.104.059055;
RA Hisamatsu T., King R.W., Helliwell C.A., Koshioka M.;
RT "The involvement of gibberellin 20-oxidase genes in phytochrome-regulated
RT petiole elongation of Arabidopsis.";
RL Plant Physiol. 138:1106-1116(2005).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION 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 [14]
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 [15]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 [16]
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 into the bioactives gibberellins GA4 and GA1, respectively.
CC Involved in the production of bioactive GA for vegetative growth and
CC development. {ECO:0000269|PubMed:16460513, ECO:0000269|PubMed:9625708,
CC ECO:0000269|PubMed:9836749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A9 + O2 = CO2 + gibberellin A4 +
CC succinate; Xref=Rhea:RHEA:68996, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:73251, ChEBI:CHEBI:73255;
CC Evidence={ECO:0000269|PubMed:9625708};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68997;
CC Evidence={ECO:0000305|PubMed:9625708};
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:9625708};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10105;
CC Evidence={ECO:0000305|PubMed:9625708};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 uM for GA9 {ECO:0000269|PubMed:9625708};
CC KM=15 uM for GA20 {ECO:0000269|PubMed:9625708};
CC KM=1.25 uM for GA9 {ECO:0000269|PubMed:15181202};
CC KM=10 uM for GA20 {ECO:0000269|PubMed:15181202};
CC Vmax=6.8 pmol/min/mg enzyme with GA9 as substrate
CC {ECO:0000269|PubMed:9625708};
CC Vmax=2.8 pmol/min/mg enzyme with GA20 as substrate
CC {ECO:0000269|PubMed:9625708};
CC Vmax=800 nmol/min/mg enzyme with GA9 as substrate
CC {ECO:0000269|PubMed:15181202};
CC Vmax=62 nmol/min/mg enzyme with GA20 as substrate
CC {ECO:0000269|PubMed:15181202};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15181202};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- INTERACTION:
CC Q39103; Q17TI5: BRX; NbExp=5; IntAct=EBI-4426378, EBI-4426649;
CC Q39103; Q9FYK5: ESR2; NbExp=5; IntAct=EBI-4426378, EBI-1536925;
CC Q39103; Q9XFM0: IAA28; NbExp=5; IntAct=EBI-4426378, EBI-3133404;
CC Q39103; Q9FUA4: SPT; NbExp=3; IntAct=EBI-4426378, EBI-1536703;
CC Q39103; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-4426378, EBI-15192297;
CC Q39103; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4426378, EBI-4426557;
CC Q39103; Q9LVG2: TOE2; NbExp=4; IntAct=EBI-4426378, EBI-4424568;
CC -!- TISSUE SPECIFICITY: Expressed in stems, roots, leaves, flowers, and
CC siliques. Highly expressed near the nodes in stems and in the stamen
CC filaments of flowers. Detected in developing cotyledons, vegetative
CC shoot apical meristem and non-meristematic, non-elongation regions of
CC the roots. Found in the cortex and the endodermis of the embryo axis in
CC germinating seeds and in the placenta in developing siliques.
CC {ECO:0000269|PubMed:11737781, ECO:0000269|PubMed:15927942,
CC ECO:0000269|PubMed:16460513, ECO:0000269|PubMed:17277098,
CC ECO:0000269|PubMed:7756830}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinating seeds and in very young
CC seedlings. Expressed in developing siliques 3-13 days after
CC pollination. {ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:9836749}.
CC -!- INDUCTION: Inhibited by GA3, indicating the existence of a probable
CC feedback loop. Inhibited by dihydro gibberellins. Regulated by
CC phytochrome. Induced sharply after red light pulse with a peak at 4
CC hours, and then decreases rapidly as germination occurs. Increases
CC again when etiolated seedling growth begins. Not regulated by long day
CC exposure or auxin. Up-regulated by cold treatment, paclobutrazol and
CC uniconazole P. {ECO:0000269|PubMed:14729916,
CC ECO:0000269|PubMed:15923331, ECO:0000269|PubMed:16905669,
CC ECO:0000269|PubMed:17277098, ECO:0000269|PubMed:7756830,
CC ECO:0000269|PubMed:9836749}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf. Ga3ox1 and ga3ox2 double mutant has a
CC severe defect in seed germination and root growth, and a dwarf
CC phenotype. {ECO:0000269|PubMed:16460513, ECO:0000269|PubMed:7756830}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
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DR EMBL; L37126; AAC37506.1; -; mRNA.
DR EMBL; AC013453; AAF71980.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29335.1; -; Genomic_DNA.
DR EMBL; BT005827; AAO64762.1; -; mRNA.
DR EMBL; AK227590; BAE99582.1; -; mRNA.
DR PIR; D86289; D86289.
DR RefSeq; NP_173008.1; NM_101424.3.
DR AlphaFoldDB; Q39103; -.
DR SMR; Q39103; -.
DR BioGRID; 23365; 10.
DR IntAct; Q39103; 8.
DR STRING; 3702.AT1G15550.1; -.
DR PaxDb; Q39103; -.
DR PRIDE; Q39103; -.
DR EnsemblPlants; AT1G15550.1; AT1G15550.1; AT1G15550.
DR GeneID; 838125; -.
DR Gramene; AT1G15550.1; AT1G15550.1; AT1G15550.
DR KEGG; ath:AT1G15550; -.
DR Araport; AT1G15550; -.
DR TAIR; locus:2196623; AT1G15550.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q39103; -.
DR OMA; AITWSEY; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q39103; -.
DR BioCyc; ARA:AT1G15550-MON; -.
DR BioCyc; MetaCyc:AT1G15550-MON; -.
DR BRENDA; 1.14.11.15; 399.
DR SABIO-RK; Q39103; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q39103; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39103; baseline and differential.
DR Genevisible; Q39103; AT.
DR GO; GO:0005737; C:cytoplasm; TAS:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
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:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
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 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..358
FT /note="Gibberellin 3-beta-dioxygenase 1"
FT /id="PRO_0000067313"
FT DOMAIN 204..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 299
FT /evidence="ECO:0000255"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 220
FT /note="C->Y: In ga4-1; semidwarf and deficient in active
FT gibberellins."
FT /evidence="ECO:0000269|PubMed:7756830"
SQ SEQUENCE 358 AA; 40162 MW; 26CED48F31554DEC CRC64;
MPAMLTDVFR GHPIHLPHSH IPDFTSLREL PDSYKWTPKD DLLFSAAPSP PATGENIPLI
DLDHPDATNQ IGHACRTWGA FQISNHGVPL GLLQDIEFLT GSLFGLPVQR KLKSARSETG
VSGYGVARIA SFFNKQMWSE GFTITGSPLN DFRKLWPQHH LNYCDIVEEY EEHMKKLASK
LMWLALNSLG VSEEDIEWAS LSSDLNWAQA ALQLNHYPVC PEPDRAMGLA AHTDSTLLTI
LYQNNTAGLQ VFRDDLGWVT VPPFPGSLVV NVGDLFHILS NGLFKSVLHR ARVNQTRARL
SVAFLWGPQS DIKISPVPKL VSPVESPLYQ SVTWKEYLRT KATHFNKALS MIRNHREE
