G2OX5_ORYSJ
ID G2OX5_ORYSJ Reviewed; 341 AA.
AC Q8LGZ9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 5 {ECO:0000305};
DE EC=1.14.11.13 {ECO:0000305|PubMed:18952778};
DE AltName: Full=Gibberellin 2-beta-hydroxylase 5 {ECO:0000305};
DE AltName: Full=Gibberellin 2-oxidase 5 {ECO:0000303|PubMed:18952778};
DE Short=GA 2-oxidase 5 {ECO:0000303|PubMed:18952778};
DE Short=OsGA2ox5 {ECO:0000303|PubMed:18952778};
GN Name=GA2OX5 {ECO:0000303|PubMed:18952778};
GN OrderedLocusNames=Os07g0103500 {ECO:0000312|EMBL:BAF20604.1},
GN LOC_Os07g01340 {ECO:0000305};
GN ORFNames=P0446F04.116 {ECO:0000312|EMBL:BAC10398.1};
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, 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24475234; DOI=10.1371/journal.pone.0087110;
RA Shan C., Mei Z., Duan J., Chen H., Feng H., Cai W.;
RT "OsGA2ox5, a gibberellin metabolism enzyme, is involved in plant growth,
RT the root gravity response and salt stress.";
RL PLoS ONE 9:E87110-E87110(2014).
CC -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of several biologically
CC active gibberellins (GAs), leading to the homeostatic regulation of
CC their endogenous level (PubMed:18952778, PubMed:24475234). Catabolism
CC of GAs plays a central role in plant development (PubMed:18952778,
CC PubMed:24475234). In vitro, converts GA12 and GA53 to the corresponding
CC 2-beta-hydroxylated products GA110 and GA97, respectively
CC (PubMed:18952778). {ECO:0000269|PubMed:18952778,
CC ECO:0000269|PubMed:24475234}.
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 -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24475234}. Nucleus
CC {ECO:0000269|PubMed:24475234}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, culms, leaf sheaths and
CC young panicles. {ECO:0000269|PubMed:24475234}.
CC -!- MISCELLANEOUS: Plant overexpressing GA2OX5 exhibit an extremely dwarf
CC phenotype. {ECO:0000269|PubMed:18952778, ECO:0000269|PubMed:24475234}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP005187; BAC10398.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20604.1; -; Genomic_DNA.
DR EMBL; AP014963; BAS99697.1; -; Genomic_DNA.
DR RefSeq; XP_015645542.1; XM_015790056.1.
DR RefSeq; XP_015645543.1; XM_015790057.1.
DR RefSeq; XP_015645544.1; XM_015790058.1.
DR RefSeq; XP_015645545.1; XM_015790059.1.
DR RefSeq; XP_015645546.1; XM_015790060.1.
DR AlphaFoldDB; Q8LGZ9; -.
DR SMR; Q8LGZ9; -.
DR STRING; 4530.OS07T0103500-01; -.
DR PaxDb; Q8LGZ9; -.
DR PRIDE; Q8LGZ9; -.
DR EnsemblPlants; Os07t0103500-01; Os07t0103500-01; Os07g0103500.
DR GeneID; 4342182; -.
DR Gramene; Os07t0103500-01; Os07t0103500-01; Os07g0103500.
DR KEGG; osa:4342182; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_15_1_1; -.
DR InParanoid; Q8LGZ9; -.
DR OMA; PESYRWG; -.
DR OrthoDB; 622449at2759; -.
DR PlantReactome; R-OSA-1119294; Gibberellin biosynthesis III (early C-13 hydroxylation).
DR PlantReactome; R-OSA-1119377; Gibberellin biosynthesis II (early C-3 hydroxylation).
DR PlantReactome; R-OSA-1119625; Gibberellin biosynthesis I (non C-3, non C-13 hydroxylation).
DR UniPathway; UPA00390; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
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:0052635; F:C-20 gibberellin 2-beta-dioxygenase activity; IEA:EnsemblPlants.
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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..341
FT /note="Gibberellin 2-beta-dioxygenase 5"
FT /id="PRO_0000445476"
FT DOMAIN 187..290
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 198
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 271
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 281
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 283
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 341 AA; 38694 MW; DCB91809DFEE99B3 CRC64;
MEEHDYDSNS NPPLMSTYKH LFVEQHRLDM DMGAIDVDEC ELPVIDLAGL MEAEQVCRAD
MVRAASEWGF FQVTNHGVPQ ALLRELHDAQ VAVFRRPFQE KVTERLLGFS PESYRWGTPT
AKCLEQLSWS EAYHIPMTTP RPSTSIRARA VIEEVSRAMY ELAQKLAEIL MRGLPGAGEG
ETMVTTREET CFLRLNRYPP CAMAMGGFGL CPHTDSDLLT IVHQQQDTVG GLQLLKGGRW
VAVKPSPSTL IVNVGDLLQA WSNDVYKSVE HRVMANATLE RFSMAFFLCP SYHTLIIPSS
SHVHDDDAHY RSFTFGEYRK QIMEDVRSTG RKIGLHRFRT R
