GAOX3_ORYSJ
ID GAOX3_ORYSJ Reviewed; 367 AA.
AC Q69LD8;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Gibberellin 20 oxidase 3 {ECO:0000305};
DE Short=OsGA20ox3 {ECO:0000303|PubMed:22992000};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O04705};
DE AltName: Full=GA 20-oxidase 3 {ECO:0000305};
DE AltName: Full=Gibberellin C-20 oxidase 3 {ECO:0000305};
GN Name=GA20OX3 {ECO:0000303|PubMed:22992000};
GN OrderedLocusNames=Os07g0169700 {ECO:0000312|EMBL:BAF20901.1},
GN LOC_Os07g07420 {ECO:0000305};
GN ORFNames=OSJNBa0050F10.19 {ECO:0000312|EMBL:BAD31785.1};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22992000; DOI=10.1094/mpmi-05-12-0138-r;
RA Qin X., Liu J.H., Zhao W.S., Chen X.J., Guo Z.J., Peng Y.L.;
RT "Gibberellin 20-oxidase gene OsGA20ox3 regulates plant stature and disease
RT development in rice.";
RL Mol. Plant Microbe Interact. 26:227-239(2013).
CC -!- FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin.
CC Catalyzes the formation of bioactive gibberellins (GAs) via a three-
CC step oxidation at C-20 of the GA skeleton. Controls the elongation of
CC the vegetative shoot and plant height by the regulation of active
CC gibberellin levels. {ECO:0000269|PubMed:22992000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + gibberellin A12 + H(+) + 3 O2 = 3 CO2 +
CC gibberellin A9 + 2 H2O + 2 succinate; 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=2 2-oxoglutarate + gibberellin A53 + H(+) + 3 O2 = 3 CO2 +
CC gibberellin A20 + 2 H2O + 2 succinate; 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;
CC Evidence={ECO:0000255|PROSITE-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; Evidence={ECO:0000305};
CC -!- MISCELLANEOUS: Plants silencing GA20OX3 exhibit a semi-dwarf phenotype,
CC and show enhanced resistance against the fungal pathogen Magnaporthe
CC oryzae and the bacterial pathogen Xanthomonas oryzae pv. oryzae, and
CC increased expression of defense-related genes. Plants over-expressing
CC GA20OX3 exhibit a elongated shoot and internode phenotype, and show
CC enhanced susceptibility against the fungal pathogen Magnaporthe oryzae
CC and the bacterial pathogen Xanthomonas oryzae pv. oryzae, and
CC accumulation of the bioactive gibberellins GA1 and GA4.
CC {ECO:0000269|PubMed:22992000}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP005840; BAD31785.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20901.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00232.1; -; Genomic_DNA.
DR AlphaFoldDB; Q69LD8; -.
DR SMR; Q69LD8; -.
DR STRING; 4530.OS07T0169700-00; -.
DR PaxDb; Q69LD8; -.
DR PRIDE; Q69LD8; -.
DR EnsemblPlants; Os07t0169700-01; Os07t0169700-01; Os07g0169700.
DR Gramene; Os07t0169700-01; Os07t0169700-01; Os07g0169700.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q69LD8; -.
DR OMA; PGESHGY; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0045544; F:gibberellin 20-oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009685; P:gibberellin metabolic process; IC:Gramene.
DR GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; 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; Plant defense;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Gibberellin 20 oxidase 3"
FT /id="PRO_0000445032"
FT DOMAIN 198..304
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 208
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 295
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 297
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 367 AA; 40495 MW; 6C6EECC6366C3409 CRC64;
MAAVVFDAAI LSKQEAIPAQ FVWPADEAPA ADDGVVEEIA IPVVDLAAFL ASGGIGRDVA
EACERHGFFQ VVNHGVDPAL LAEAYRCCDA FYARPLAEKQ RARRRPGENH GYASSFTGRF
DCKLPWKETM SFNCSAAPGN ARMVADYFVD ALGEEYRHMG EVYQEYCDVM TRLALDVTEV
LAVALGLGRG ELRGFFADGD PVMRLNHYPP CRQPHLTLGT GPHRDPTSLT LLHQDDVGGL
QVLPDDAAAA AGGWRAVRPR ADAFVVNIGD TFAALTNGRH ASCLHRAVVN GRVARRSLTF
FLNPRLDRVV SPPPALVDAA HPRAFPDFTW REFLEFTQRH YRSDTNTMDA FVAWIKQRNG
YESLDKY
