G2OX1_ORYSJ
ID G2OX1_ORYSJ Reviewed; 382 AA.
AC Q5W726; Q9AVA5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 1 {ECO:0000305};
DE EC=1.14.11.13 {ECO:0000269|PubMed:11244129};
DE AltName: Full=Gibberellin 2-beta-hydroxylase 1 {ECO:0000305};
DE AltName: Full=Gibberellin 2-oxidase 1 {ECO:0000303|PubMed:11244129};
DE Short=GA 2-oxidase 1 {ECO:0000303|PubMed:11244129};
DE Short=OsGA2ox1 {ECO:0000303|PubMed:11244129};
GN Name=GA2OX1 {ECO:0000303|PubMed:11244129};
GN OrderedLocusNames=Os05g0158600 {ECO:0000312|EMBL:BAF16625.1},
GN LOC_Os05g06670 {ECO:0000305};
GN ORFNames=OSJNBa0017J22.4 {ECO:0000312|EMBL:AAV43914.1};
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, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=11244129; DOI=10.1104/pp.125.3.1508;
RA Sakamoto T., Kobayashi M., Itoh H., Tagiri A., Kayano T., Tanaka H.,
RA Iwahori S., Matsuoka M.;
RT "Expression of a gibberellin 2-oxidase gene around the shoot apex is
RT related to phase transition in rice.";
RL Plant Physiol. 125:1508-1516(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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).
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. Controls the level of bioactive GAs in the shoot
CC apical meristem, which regulates the vegetative to reproductive phase
CC transition. In vitro, converts GA1, GA4, GA9, GA20, and GA44 to the
CC corresponding 2-beta-hydroxylated products GA8, GA34, GA51, GA29, and
CC GA98, respectively. {ECO:0000269|PubMed:11244129}.
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:11244129};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:11244129};
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, and in the basal
CC region of leaf primordia and young leaves.
CC {ECO:0000269|PubMed:11244129}.
CC -!- MISCELLANEOUS: Plants overexpressing GA2OX1 exhibit extremely dwarf
CC phenotype and are unable to achieve phase transition from vegetative to
CC reproductive growth. {ECO:0000269|PubMed:11244129}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
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DR EMBL; AB059416; BAB40934.1; -; mRNA.
DR EMBL; AC119288; AAV43914.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16625.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92384.1; -; Genomic_DNA.
DR RefSeq; XP_015639483.1; XM_015783997.1.
DR AlphaFoldDB; Q5W726; -.
DR SMR; Q5W726; -.
DR STRING; 4530.OS05T0158600-01; -.
DR PaxDb; Q5W726; -.
DR PRIDE; Q5W726; -.
DR EnsemblPlants; Os05t0158600-02; Os05t0158600-02; Os05g0158600.
DR GeneID; 4337874; -.
DR Gramene; Os05t0158600-02; Os05t0158600-02; Os05g0158600.
DR KEGG; osa:4337874; -.
DR InParanoid; Q5W726; -.
DR OrthoDB; 622449at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q5W726; baseline and differential.
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:0102111; F:gibberellin A20,2-oxoglutarate:oxygen oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0102924; F:gibberellin A44,2-oxoglutarate:oxygen oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0102652; F:gibberellin A9,2-oxoglutarate:oxygen oxidoreductase 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 Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Gibberellin 2-beta-dioxygenase 1"
FT /id="PRO_0000444355"
FT DOMAIN 189..321
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 199
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 312
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 314
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 382 AA; 40620 MW; F6B1EE97E7982AD6 CRC64;
MVVPSATTPA RQETVVAAAP PAAAASGVVG GGGGVTIATV DMSAERGAVA RQVATACAAH
GFFRCVGHGV PAAAPVAARL DAATAAFFAM APAEKQRAGP ASPLGYGCRS IGFNGDVGEL
EYLLLHANPA AVAHRARTID AMDPSRFSAI VNEYIEAMKK LACEILDLLG EGLGLKDPRY
FSKLTTNADS DCLLRINHYP PSCNIHKLDH DDQCNIKSLV STKASNGGNL MAGGRIGFGE
HSDPQILSLL RANDVEGLQV FVPDHEGKEM WVQVPSDPSA IFVNVGDVLQ ALTNGRLISI
RHRVIATACR PRLSTIYFAS PPLHARISAL PETITASSPR RYRSFTWAEY KTTMYSLRLS
HSRLELFKID DDDSDNASEG KA
