G2OX3_ORYSJ
ID G2OX3_ORYSJ Reviewed; 327 AA.
AC Q8S0S6;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 3 {ECO:0000305};
DE EC=1.14.11.13 {ECO:0000269|PubMed:12736788};
DE AltName: Full=Gibberellin 2-beta-hydroxylase 3 {ECO:0000305};
DE AltName: Full=Gibberellin 2-oxidase 3 {ECO:0000303|PubMed:12736788};
DE Short=GA 2-oxidase 3 {ECO:0000303|PubMed:12736788};
DE Short=OsGA2ox3 {ECO:0000303|PubMed:12736788};
GN Name=GA2OX3 {ECO:0000303|PubMed:12736788};
GN OrderedLocusNames=Os01g0757200 {ECO:0000312|EMBL:BAF06206.1},
GN LOC_Os01g55240 {ECO:0000305};
GN ORFNames=OJ1414_E05.17 {ECO:0000312|EMBL:BAB90150.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP TISSUE SPECIFICITY, AND INDUCTION BY GIBBERELLIN.
RC STRAIN=cv. Nipponbare;
RX PubMed=12736788; DOI=10.1007/s10265-003-0080-z;
RA Sakai M., Sakamoto T., Saito T., Matsuoka M., Tanaka H., Kobayashi M.;
RT "Expression of novel rice gibberellin 2-oxidase gene is under homeostatic
RT regulation by biologically active gibberellins.";
RL J. Plant Res. 116:161-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION.
RX PubMed=18952778; DOI=10.1105/tpc.108.060913;
RA Lo S.F., Yang S.Y., Chen K.T., Hsing Y.I., Zeevaart J.A., Chen L.J.,
RA Yu S.M.;
RT "A novel class of gibberellin 2-oxidases control semidwarfism, tillering,
RT and root development in rice.";
RL Plant Cell 20:2603-2618(2008).
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 (PubMed:12736788, PubMed:18952778). In vitro,
CC converts GA1, GA20, and GA29 to the corresponding 2-beta-hydroxylated
CC products GA8, GA29-catabolite, respectively (PubMed:12736788).
CC {ECO:0000269|PubMed:12736788, ECO:0000269|PubMed:18952778}.
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 Evidence={ECO:0000269|PubMed:12736788};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:12736788};
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 -!- TISSUE SPECIFICITY: Expressed in roots, shoot apex, leaf blades, leaf
CC sheaths, stems and flowers. {ECO:0000269|PubMed:12736788}.
CC -!- INDUCTION: Induced by gibberellin. {ECO:0000269|PubMed:12736788}.
CC -!- MISCELLANEOUS: Plants overexpressing GA2OX3 exhibit extremely dwarf
CC phenotype and are unable to achieve phase transition from vegetative to
CC reproductive growth. {ECO:0000269|PubMed:12736788,
CC ECO:0000269|PubMed:18952778}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
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DR EMBL; AB092485; BAC16752.1; -; mRNA.
DR EMBL; AP003375; BAB90150.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06206.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74413.1; -; Genomic_DNA.
DR EMBL; AK060666; BAG87530.1; -; mRNA.
DR EMBL; AK060714; BAG87549.1; -; mRNA.
DR EMBL; AK101713; BAG95200.1; -; mRNA.
DR RefSeq; XP_015649346.1; XM_015793860.1.
DR PDB; 6KU3; X-ray; 2.15 A; A/B/C/D=1-327.
DR PDBsum; 6KU3; -.
DR AlphaFoldDB; Q8S0S6; -.
DR SMR; Q8S0S6; -.
DR STRING; 4530.OS01T0757200-01; -.
DR PaxDb; Q8S0S6; -.
DR PRIDE; Q8S0S6; -.
DR EnsemblPlants; Os01t0757200-01; Os01t0757200-01; Os01g0757200.
DR GeneID; 4325145; -.
DR Gramene; Os01t0757200-01; Os01t0757200-01; Os01g0757200.
DR KEGG; osa:4325145; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q8S0S6; -.
DR OMA; ANGMESR; -.
DR OrthoDB; 622449at2759; -.
DR BioCyc; MetaCyc:MON-840; -.
DR PlantReactome; R-OSA-9631623; Regulation of embryo development.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
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:0045543; F:gibberellin 2-beta-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045487; P:gibberellin catabolic process; IBA:GO_Central.
DR GO; GO:0009685; P:gibberellin metabolic process; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; 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 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..327
FT /note="Gibberellin 2-beta-dioxygenase 3"
FT /id="PRO_0000444357"
FT DOMAIN 173..278
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 183
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 269
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 271
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:6KU3"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 129..156
FT /evidence="ECO:0007829|PDB:6KU3"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:6KU3"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6KU3"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:6KU3"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6KU3"
SQ SEQUENCE 327 AA; 35326 MW; 650793027ACA6FCE CRC64;
MVVLAGPPAV DHIPLLRSPD PGDVFSGVPV VDLGSPGAAR AVVDACERYG FFKVVNHGVA
TDTMDKAESE AVRFFSQTQP DKDRSGPAYP FGYGSKRIGF NGDMGWLEYL LLALDDASLA
DACTVPSCAV FRAALNEYIS GVRKVAVRVM EAMSEGLGIA QADALSALVT AEGSDQVFRV
NHYPPCRALQ GLGCSVTGFG EHTDPQLVSV LRSNGTSGLQ IALRDGQWVS VPSDRDSFFV
NVGDSLQVLT NGRFKSVKHR VVANSLKSRV SFIYFGGPPL AQRIAPLPQL LGEGEQSLYK
EFTWDEYKKA AYKSRLGDNR LAQFEKK
