ID GAOX1_ORYSJ Reviewed; 372 AA. AC P93771; Q10AC7; Q84M83; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2018, sequence version 3. DT 02-SEP-2026, entry version 128. DE RecName: Full=Gibberellin 20 oxidase 1 {ECO:0000303|PubMed:12834406}; DE Short=OsGA20ox1 {ECO:0000303|PubMed:12834406}; DE EC=1.14.11.- {ECO:0000305}; DE AltName: Full=GA 20-oxidase 1 {ECO:0000303|PubMed:12834406}; DE AltName: Full=Gibberellin C-20 oxidase 1 {ECO:0000305}; DE AltName: Full=Os20ox {ECO:0000303|Ref.1}; GN Name=GA20OX1 {ECO:0000305}; GN Synonyms=20ox1 {ECO:0000305}, GA20ox-1 {ECO:0000305}; GN OrderedLocusNames=Os03g0856700 {ECO:0000312|EMBL:BAF13865.1}, GN LOC_Os03g63970 {ECO:0000312|EMBL:ABF99990.1}; GN ORFNames=OSJNBa0059G06.22 {ECO:0000312|EMBL:AAP21386.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION. RC STRAIN=cv. Nipponbare; RX DOI=10.1111/j.1399-3054.1997.tb03438.x; RA Toyomasu T., Kawaide H., Sekimoto H., von Numers C., Phillips A.L., RA Hedden P., Kamiya Y.; RT "Cloning and characterization of a cDNA encoding gibberellin 20-oxidase RT from rice (Oryza sativa) seedlings."; RL Physiol. Plantarum 99:111-118(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [6] RP TISSUE SPECIFICITY. RX PubMed=11961544; DOI=10.1038/416701a; RA Sasaki A., Ashikari M., Ueguchi-Tanaka M., Itoh H., Nishimura A., RA Swapan D., Ishiyama K., Saito T., Kobayashi M., Khush G.S., Kitano H., RA Matsuoka M.; RT "A mutant gibberellin-synthesis gene in rice."; RL Nature 416:701-702(2002). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12834406; DOI=10.1046/j.1365-313x.2003.01780.x; RA Kaneko M., Itoh H., Inukai Y., Sakamoto T., Ueguchi-Tanaka M., Ashikari M., RA Matsuoka M.; RT "Where do gibberellin biosynthesis and gibberellin signaling occur in rice RT plants?"; RL Plant J. 35:104-115(2003). RN [8] RP FUNCTION. RX PubMed=15604710; DOI=10.1007/s11103-004-1692-y; RA Oikawa T., Koshioka M., Kojima K., Yoshida H., Kawata M.; RT "A role of OsGA20ox1, encoding an isoform of gibberellin 20-oxidase, for RT regulation of plant stature in rice."; RL Plant Mol. Biol. 55:687-700(2004). CC -!- FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin CC (PubMed:15604710, Ref.1). Catalyzes the conversion of GA12 and GA53 to CC GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA CC skeleton (Ref.1). {ECO:0000269|PubMed:15604710, ECO:0000269|Ref.1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=gibberellin A12 + 2 2-oxoglutarate + 3 O2 + H(+) = gibberellin CC A9 + 2 succinate + 3 CO2 + 2 H2O; Xref=Rhea:RHEA:60772, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:58627, ChEBI:CHEBI:73255; CC Evidence={ECO:0000250|UniProtKB:O04705}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773; CC Evidence={ECO:0000250|UniProtKB:O04705}; CC -!- CATALYTIC ACTIVITY: CC Reaction=gibberellin A53 + 2 2-oxoglutarate + 3 O2 + H(+) = gibberellin CC A20 + 2 succinate + 3 CO2 + 2 H2O; Xref=Rhea:RHEA:60796, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:58526, ChEBI:CHEBI:143954; CC Evidence={ECO:0000250|UniProtKB:O04705}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797; CC Evidence={ECO:0000250|UniProtKB:O04705}; 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 -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC -!- TISSUE SPECIFICITY: Preferentially expressed in reproductive organs CC (PubMed:11961544). Expressed in the epithelium of embryos and the CC tapetum of anthers. Expressed at low levels in the shoot apical CC meristem (PubMed:12834406). {ECO:0000269|PubMed:11961544, CC ECO:0000269|PubMed:12834406}. CC -!- INDUCTION: Negatively controlled by the level of physiologically active CC gibberellin. {ECO:0000269|Ref.1}. CC -!- MISCELLANEOUS: Plants over-expressing GA20OX1 have high levels of CC bioactive gibberellins, and exhibit an overgrowth phenotype with CC increased internode elongation and leaf sheath length CC (PubMed:15604710). Plant silencing GA20OX1 exhibit a semi-dwarf CC phenotype (PubMed:15604710). {ECO:0000269|PubMed:15604710}. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. GA20OX subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP21386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U50333; AAB48239.1; -; mRNA. DR EMBL; AC096690; AAP21386.1; ALT_INIT; Genomic_DNA. DR EMBL; DP000009; ABF99990.1; -; Genomic_DNA. DR EMBL; AP008209; BAF13865.1; -; Genomic_DNA. DR EMBL; AP014959; BAS87451.1; -; Genomic_DNA. DR EMBL; AK099111; BAG93931.1; -; mRNA. DR PIR; T04337; T04337. DR AlphaFoldDB; P93771; -. DR SMR; P93771; -. DR FunCoup; P93771; 90. DR STRING; 39947.P93771; -. DR PaxDb; 39947-P93771; -. DR EnsemblPlants; Os03t0856700-01; Os03t0856700-01; Os03g0856700. DR EnsemblPlants; Os03t0856700-02; Os03t0856700-02; Os03g0856700. DR Gramene; Os03t0856700-01; Os03t0856700-01; Os03g0856700. DR Gramene; Os03t0856700-02; Os03t0856700-02; Os03g0856700. DR KEGG; dosa:Os03g0856700; -. DR KEGG; osa:4334841; -. DR eggNOG; KOG0143; Eukaryota. DR HOGENOM; CLU_010119_16_3_1; -. DR InParanoid; P93771; -. DR OMA; SQFIWPA; -. DR OrthoDB; 288590at2759; -. DR BRENDA; 1.14.11.13; 4460. DR Proteomes; UP000059680; Chromosome 3. DR GO; GO:0045544; F:gibberellin 20-oxidase activity; IEA:RHEA. DR GO; GO:0009685; P:gibberellin metabolic process; IC:Gramene. DR FunFam; 2.60.120.330:FF:000003; Gibberellin 20 oxidase 2; 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 Iron; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..372 FT /note="Gibberellin 20 oxidase 1" FT /id="PRO_0000219517" FT DOMAIN 209..309 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT ACT_SITE 300 FT /evidence="ECO:0000255" FT BINDING 234 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 236 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 290 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT CONFLICT 107..116 FT /note="AQRRAGESCG -> RSGARGRTA (in Ref. 1; AAB48239)" FT /evidence="ECO:0000305" FT CONFLICT 352..353 FT /note="TL -> LF (in Ref. 1; AAB48239)" FT /evidence="ECO:0000305" SQ SEQUENCE 372 AA; 42256 MW; 6BC532897F731C27 CRC64; MSMVVQQEQE VVFDAAVLSG QTEIPSQFIW PAEESPGSVA VEELEVALID VGAGAERSSV VRQVGEACER HGFFLVVNHG IEAALLEEAH RCMDAFFTLP LGEKQRAQRR AGESCGYASS FTGRFASKLP WKETLSFRYS SAGDEEGEEG VGEYLVRKLG AEHGRRLGEV YSRYCHEMSR LSLELMEVLG ESLGIVGDRR HYFRRFFQRN DSIMRLNYYP ACQRPLDTLG TGPHCDPTSL TILHQDHVGG LEVWAEGRWR AIRPRPGALV VNVGDTFMAL SNARYRSCLH RAVVNSTAPR RSLAFFLCPE MDTVVRPPEE LVDDHHPRVY PDFTWRALLD FTQRHYRADM RTLQAFSDWL NHHRHLQPTI YS //