G3OX2_ORYSJ
ID G3OX2_ORYSJ Reviewed; 373 AA.
AC Q9FU53; Q0JQ78;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 2 {ECO:0000305};
DE EC=1.14.11.15 {ECO:0000269|PubMed:11438692};
DE AltName: Full=GA 3-oxidase 2 {ECO:0000305};
DE Short=OsGA3ox2 {ECO:0000303|PubMed:11438692};
DE AltName: Full=Gibberellin 3 beta-hydroxylase 2 {ECO:0000303|PubMed:11438692};
DE AltName: Full=Protein DWARF18 {ECO:0000303|PubMed:11438692};
GN Name=GA3OX2 {ECO:0000303|PubMed:11438692};
GN Synonyms=D18 {ECO:0000303|PubMed:11438692};
GN OrderedLocusNames=Os01g0177400 {ECO:0000312|EMBL:BAS70691.1},
GN LOC_Os01g08220 {ECO:0000305};
GN ORFNames=OsJ_00594 {ECO:0000312|EMBL:EAZ10757.1},
GN P0013F10.29 {ECO:0000312|EMBL:BAB17075.1};
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, CATALYTIC ACTIVITY, COFACTOR, TISSUE
RP SPECIFICITY, INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Hoshinoyume, and cv. Nipponbare; TISSUE=Shoot;
RX PubMed=11438692; DOI=10.1073/pnas.141239398;
RA Itoh H., Ueguchi-Tanaka M., Sentoku N., Kitano H., Matsuoka M.,
RA Kobayashi M.;
RT "Cloning and functional analysis of two gibberellin 3 beta - hydroxylase
RT genes that are differently expressed during the growth of rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8909-8914(2001).
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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP FUNCTION.
RX DOI=10.1270/jsbbs.52.215;
RA Itoh H., Ueguchi-Tanaka M., Sakamoto T., Kayano T., Tanaka H., Ashikari M.,
RA Matsuoka M.;
RT "Modification of rice plant height by suppressing the height-controlling
RT gene, D18, in rice.";
RL Breed. Sci. 52:215-218(2002).
CC -!- FUNCTION: Catalyzes the 3-beta-hydroxylation of the inactive
CC gibberellin precursors, leading to the formation of bioactive
CC gibberellins. In vitro, converts the precursors GA20, GA5, GA44 and GA9
CC to the corresponding 3-beta-hydroxylated active products GA1, GA3, GA38
CC and GA4, respectively. Involved in the production of bioactive GA for
CC vegetative growth and development (PubMed:11438692). Controls the
CC elongation of the vegetative shoot and plant height by the regulation
CC of active gibberellin levels (Ref.7). {ECO:0000269|PubMed:11438692,
CC ECO:0000269|Ref.7}.
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:11438692};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:11438692};
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 -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in elongating leaves. Expressed in
CC unopened flowers. Expressed at low levels in leaf blades, shoots,
CC rachis, stems and young panicles. {ECO:0000269|PubMed:11438692}.
CC -!- DEVELOPMENTAL STAGE: During anther development, expressed in the
CC tapetum at the early-stage and middle-stage of pollen differentiation.
CC {ECO:0000269|PubMed:11438692}.
CC -!- INDUCTION: Induced by uniconazole. Down-regulated by gibberellin (GA3).
CC {ECO:0000269|PubMed:11438692}.
CC -!- MISCELLANEOUS: Plants silencing G3OX2 exhibit reduced plant height.
CC {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF04100.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS70691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB056519; BAB62155.1; -; mRNA.
DR EMBL; AB269821; BAF03047.1; -; mRNA.
DR EMBL; AP002523; BAB17075.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04100.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS70691.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000138; EAZ10757.1; -; Genomic_DNA.
DR RefSeq; XP_015634638.1; XM_015779152.1.
DR PDB; 7EKD; X-ray; 1.90 A; A=1-373.
DR PDBsum; 7EKD; -.
DR AlphaFoldDB; Q9FU53; -.
DR SMR; Q9FU53; -.
DR STRING; 4530.OS01T0177400-01; -.
DR GeneID; 4323864; -.
DR KEGG; osa:4323864; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9FU53; -.
DR OrthoDB; 622449at2759; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009685; P:gibberellin metabolic process; IC:Gramene.
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..373
FT /note="Gibberellin 3-beta-dioxygenase 2"
FT /id="PRO_0000445031"
FT DOMAIN 203..304
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 212
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 229
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 373 AA; 40572 MW; 2075DBFCAE5F6017 CRC64;
MPTPSHLKNP LCFDFRAARR VPETHAWPGL DDHPVVDGGG GGGEDAVPVV DVGAGDAAAR
VARAAEQWGA FLLVGHGVPA ALLSRVEERV ARVFSLPASE KMRAVRGPGE PCGYGSPPIS
SFFSKLMWSE GYTFSPSSLR SELRRLWPKS GDDYLLFCDV MEEFHKEMRR LADELLRLFL
RALGLTGEEV AGVEAERRIG ERMTATVHLN WYPRCPEPRR ALGLIAHTDS GFFTFVLQSL
VPGLQLFRRG PDRWVAVPAV AGAFVVNVGD LFHILTNGRF HSVYHRAVVN RDRDRVSLGY
FLGPPPDAEV APLPEAVPAG RSPAYRAVTW PEYMAVRKKA FATGGSALKM VSTDAAAAAD
EHDDVAAAAD VHA
