G3OX1_ORYSJ
ID G3OX1_ORYSJ Reviewed; 384 AA.
AC Q6AT12; A0A0P0WII8;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 1 {ECO:0000305};
DE EC=1.14.11.15 {ECO:0000269|PubMed:11438692};
DE AltName: Full=GA 3-oxidase 1 {ECO:0000305};
DE Short=OsGA3ox1 {ECO:0000303|PubMed:11438692};
DE AltName: Full=Gibberellin 3 beta-hydroxylase 1 {ECO:0000303|PubMed:11438692};
GN Name=GA3OX1 {ECO:0000303|PubMed:11438692};
GN OrderedLocusNames=Os05g0178100 {ECO:0000312|EMBL:BAF16712.1},
GN LOC_Os05g08540 {ECO:0000305};
GN ORFNames=OSJNBa0029B02.17 {ECO:0000312|EMBL:AAT77356.1};
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=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 [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 MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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).
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 bioactive products GA1, GA3,
CC GA38 and GA4, respectively. Involved in the production of bioactive GA
CC for vegetative growth and development. May possess 2,3-desaturase
CC activity, catalyzing the conversion of GA9 to 2,3-dehydro-GA9, and GA20
CC to GA5 (2,3-dehydro GA20). May possess 2-beta-hydroxylase activity,
CC catalyzing the conversion of GA1 and GA4 to the corresponding 2-beta-
CC hydroxylated products GA8 and GA34, respectively.
CC {ECO:0000269|PubMed:11438692}.
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: Expressed in unopened flowers.
CC {ECO:0000269|PubMed:11438692}.
CC -!- DEVELOPMENTAL STAGE: During anther development, expressed in the
CC tapetum at the middle-stage and late-stage of pollen differentiation.
CC {ECO:0000269|PubMed:11438692}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAS92534.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC144738; AAT77356.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16712.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92534.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK120915; BAH00227.1; -; mRNA.
DR RefSeq; XP_015638886.1; XM_015783400.1.
DR AlphaFoldDB; Q6AT12; -.
DR SMR; Q6AT12; -.
DR STRING; 4530.OS05T0178100-01; -.
DR GeneID; 4337968; -.
DR KEGG; osa:4337968; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q6AT12; -.
DR OrthoDB; 622449at2759; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
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 Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..384
FT /note="Gibberellin 3-beta-dioxygenase 1"
FT /id="PRO_0000445030"
FT DOMAIN 225..327
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 250
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 252
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 318
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 320
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 384 AA; 41555 MW; E2264DB9963F3AA3 CRC64;
MQIMTSSSTS PTSPTSPLAA AADNGVAAAY FNFRGAERVP ESHVWKGMHE KDTAPVAAAD
ADGGDAVPVV DMSGGDDAAV AAVARAAEEW GGFLLVGHGV TAEALARVEA QAARLFALPA
DDKARGARRP GGGNTGYGVP PYLLRYPKQM WAEGYTFPPP AIRDEFRRVW PDAGDDYHRF
CSAMEEYDSS MRALGERLLA MFFKALGLAG NDAPGGETER KIRETLTSTI HLNMFPRCPD
PDRVVGLAAH TDSGFFTFIL QSPVPGLQLL RHRPDRWVTV PGTPGALIVV VGDLFHVLTN
GRFHSVFHRA VVNRERDRIS MPYFLGPPAD MKVTPLVAAG SPESKAVYQA VTWPEYMAVR
DKLFGTNISA LSMIRVAKEE DKES
