G2OX6_ORYSJ
ID G2OX6_ORYSJ Reviewed; 358 AA.
AC Q7XP65;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 6 {ECO:0000305};
DE EC=1.14.11.13 {ECO:0000269|PubMed:18952778};
DE AltName: Full=Gibberellin 2-beta-hydroxylase 6 {ECO:0000305};
DE AltName: Full=Gibberellin 2-oxidase 6 {ECO:0000303|PubMed:18952778};
DE Short=GA 2-oxidase 6 {ECO:0000303|PubMed:18952778};
DE Short=OsGA2ox6 {ECO:0000303|PubMed:18952778};
GN Name=GA2OX6 {ECO:0000303|PubMed:18952778};
GN OrderedLocusNames=Os04g0522500 {ECO:0000312|EMBL:BAF15255.1},
GN LOC_Os04g44150 {ECO:0000305};
GN ORFNames=OsJ_15497 {ECO:0000312|EMBL:EAZ31370.1},
GN OSJNBa0019D11.23 {ECO:0000312|EMBL:CAE03751.1};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20171575; DOI=10.1016/s1673-8527(09)60022-9;
RA Huang J., Tang D., Shen Y., Qin B., Hong L., You A., Li M., Wang X., Yu H.,
RA Gu M., Cheng Z.;
RT "Activation of gibberellin 2-oxidase 6 decreases active gibberellin levels
RT and creates a dominant semi-dwarf phenotype in rice (Oryza sativa L.).";
RL J. Genet. Genomics 37:23-36(2010).
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:18952778, PubMed:20171575). In vitro,
CC converts GA12 and GA53 to the corresponding 2-beta-hydroxylated
CC products GA110 and GA97, respectively. {ECO:0000269|PubMed:18952778,
CC ECO:0000269|PubMed:20171575}.
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:18952778};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:18952778};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20171575}. Nucleus
CC {ECO:0000269|PubMed:20171575}.
CC -!- TISSUE SPECIFICITY: Expressed in panicles. Expressed at low levels in
CC young shoots, leaf blades and elongating internodes.
CC {ECO:0000269|PubMed:20171575}.
CC -!- MISCELLANEOUS: Plants overexpressing GA2OX6 exhibit extremely dwarf
CC phenotype and are unable to achieve phase transition from vegetative to
CC reproductive growth. This phenotype can be rescued by application of
CC exogenous gibberellin (GA3). {ECO:0000269|PubMed:18952778,
CC ECO:0000269|PubMed:20171575}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
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DR EMBL; AL662958; CAE03751.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF15255.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90133.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31370.1; -; Genomic_DNA.
DR RefSeq; XP_015635159.1; XM_015779673.1.
DR AlphaFoldDB; Q7XP65; -.
DR SMR; Q7XP65; -.
DR STRING; 4530.OS04T0522500-01; -.
DR PaxDb; Q7XP65; -.
DR PRIDE; Q7XP65; -.
DR EnsemblPlants; Os04t0522500-01; Os04t0522500-01; Os04g0522500.
DR GeneID; 4336431; -.
DR Gramene; Os04t0522500-01; Os04t0522500-01; Os04g0522500.
DR KEGG; osa:4336431; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_15_1_1; -.
DR InParanoid; Q7XP65; -.
DR OMA; VCHTDSD; -.
DR OrthoDB; 622449at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0052634; F:C-19 gibberellin 2-beta-dioxygenase activity; IEA:UniProtKB-EC.
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:0010336; P:gibberellic acid homeostasis; IMP:UniProtKB.
DR GO; GO:0045487; P:gibberellin catabolic process; IMP:UniProtKB.
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 Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..358
FT /note="Gibberellin 2-beta-dioxygenase 6"
FT /id="PRO_0000444358"
FT DOMAIN 207..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 218
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 235
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 BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 301
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 358 AA; 39038 MW; 80F7E9A6D58B3C2A CRC64;
MPAFADIAID PPLADSYRAL ALLRRDRDGG IAPPAVQMVG SGGAVLERDL PMVDLERLTR
GGAGERKACA GAMARAASEW GFFQLTNHGV GRELMEEMRR EQARLFRLPF ETKEKAGLLN
GSYRWGNPTA TSLRHLSWSE AFHVPLASIS GADCDFGDLT SLRGVMQEVA EAMSRVANTV
AAALAEELTG RGGGGASAAP WFPAGCDETT CFLRLNRYPA CPFAADTFGL VPHTDSDFLT
VLCQDQVGGL HLMKDSRWVA VRPRPDALVV NIGDLFQAWS NNRYKSVEHK VVANAKTDRL
SVAYFLCPSY DSLVGTCGEP SPYRAFTFGE YRKKVQEDVR TTGKKIGLPN FFKHSSVQ
