G2OX2_ORYSJ
ID G2OX2_ORYSJ Reviewed; 370 AA.
AC Q5ZA21; C7IXN0; Q8H947;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 2 {ECO:0000305};
DE EC=1.14.11.13 {ECO:0000305};
DE AltName: Full=Gibberellin 2-beta-hydroxylase 2 {ECO:0000305};
DE AltName: Full=Gibberellin 2-oxidase 2 {ECO:0000303|PubMed:12736788};
DE Short=GA 2-oxidase 2 {ECO:0000303|PubMed:12736788};
DE Short=OsGA2ox2 {ECO:0000303|PubMed:12736788};
GN Name=GA2OX2 {ECO:0000303|PubMed:12736788};
GN OrderedLocusNames=Os01g0332200 {ECO:0000312|EMBL:BAS71921.1},
GN LOC_Os01g22910 {ECO:0000305};
GN ORFNames=B1140D12.2 {ECO:0000312|EMBL:BAD53498.1};
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].
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).
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. {ECO:0000250|UniProtKB:Q5W726}.
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:0000305};
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 -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH91043.1; Type=Erroneous gene model prediction; Evidence={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; AB092484; BAC16751.1; -; Genomic_DNA.
DR EMBL; AP003537; BAD53498.1; -; Genomic_DNA.
DR EMBL; AP008207; BAH91043.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS71921.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5ZA21; -.
DR SMR; Q5ZA21; -.
DR STRING; 4530.OS01T0332200-01; -.
DR PaxDb; Q5ZA21; -.
DR PRIDE; Q5ZA21; -.
DR EnsemblPlants; Os01t0332200-01; Os01t0332200-01; Os01g0332200.
DR Gramene; Os01t0332200-01; Os01t0332200-01; Os01g0332200.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_8_1_1; -.
DR InParanoid; Q5ZA21; -.
DR OMA; ARMSMAY; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045487; P:gibberellin catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..370
FT /note="Gibberellin 2-beta-dioxygenase 2"
FT /id="PRO_0000444356"
FT DOMAIN 186..306
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 196
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 297
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT CONFLICT 80
FT /note="A -> G (in Ref. 1; BAC16751)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="V -> A (in Ref. 1; BAC16751)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..99
FT /note="PPD -> RPT (in Ref. 1; BAC16751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 38725 MW; 9222D7E071BEA83E CRC64;
MVVPAAAAPE CGRREAAAAA AAAVFCRRGR GVVVPTVDMS APAGRGELSR QVARACAGSG
FFRAVNHGVP PRVSAAMDAA AAAFFVRAGA EKQLAGPPDP LGYGSRSIGA NGDVGELEYL
ILHASPDAVA RKASAIDRED PRRFSQVVND YVEAVRQLAC HVLDLLGEGL GLRDPTSLTR
LITATDNDSL IRINHYPPSC AAAAGDHKSG GGPAPTAAIG FGEHTDPQIL SVLRANDADG
LQLLLPDAAA AGDSVWVPVP PDPSAFFVNV GDLLQALTNG RLVSIRHRVV VGTGKPRLST
IYFAAPPLHA RISALPETVA AGAPRRYRAF TWAEYKRTMY TLRLSHNRLD LFHAGDGDGD
AGVGDDDDHE
