G3OX3_ARATH
ID G3OX3_ARATH Reviewed; 349 AA.
AC Q9SVS8; A0MF88; Q1PE60;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 3;
DE EC=1.14.11.15;
DE AltName: Full=GA 3-oxidase 3;
DE Short=AtGA3ox3;
DE Short=AtGA3ox4;
DE AltName: Full=Gibberellin 3 beta-hydroxylase 3;
GN Name=GA3OX3; OrderedLocusNames=At4g21690; ORFNames=F17L22.150;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16460513; DOI=10.1111/j.1365-313x.2005.02642.x;
RA Mitchum M.G., Yamaguchi S., Hanada A., Kuwahara A., Yoshioka Y., Kato T.,
RA Tabata S., Kamiya Y., Sun T.P.;
RT "Distinct and overlapping roles of two gibberellin 3-oxidases in
RT Arabidopsis development.";
RL Plant J. 45:804-818(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17277098; DOI=10.1104/pp.106.093542;
RA Matsushita A., Furumoto T., Ishida S., Takahashi Y.;
RT "AGF1, an AT-hook protein, is necessary for the negative feedback of
RT AtGA3ox1 encoding GA 3-oxidase.";
RL Plant Physiol. 143:1152-1162(2007).
RN [6]
RP GENE FAMILY.
RX PubMed=21056641; DOI=10.1016/j.gene.2010.10.010;
RA Han F., Zhu B.;
RT "Evolutionary analysis of three gibberellin oxidase genes in rice,
RT Arabidopsis, and soybean.";
RL Gene 473:23-35(2011).
CC -!- FUNCTION: Converts the inactive gibberellin (GA) precursors GA9 and
CC GA20 in the bioactives gibberellins GA4 and GA1. Involved in the
CC production of bioactive GA for reproductive development.
CC {ECO:0000269|PubMed:16460513}.
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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in flower clusters and siliques.
CC {ECO:0000269|PubMed:16460513, ECO:0000269|PubMed:17277098}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28643.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL035527; CAB36813.1; -; Genomic_DNA.
DR EMBL; AL161555; CAB81276.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84490.1; -; Genomic_DNA.
DR EMBL; DQ446858; ABE66082.1; -; mRNA.
DR EMBL; DQ653214; ABK28643.1; ALT_SEQ; mRNA.
DR PIR; T05844; T05844.
DR RefSeq; NP_193900.1; NM_118289.1.
DR AlphaFoldDB; Q9SVS8; -.
DR SMR; Q9SVS8; -.
DR BioGRID; 13545; 1.
DR STRING; 3702.AT4G21690.1; -.
DR PaxDb; Q9SVS8; -.
DR PRIDE; Q9SVS8; -.
DR EnsemblPlants; AT4G21690.1; AT4G21690.1; AT4G21690.
DR GeneID; 828256; -.
DR Gramene; AT4G21690.1; AT4G21690.1; AT4G21690.
DR KEGG; ath:AT4G21690; -.
DR Araport; AT4G21690; -.
DR TAIR; locus:2119068; AT4G21690.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9SVS8; -.
DR OMA; KNLQIGP; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9SVS8; -.
DR BioCyc; ARA:AT4G21690-MON; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9SVS8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVS8; baseline and differential.
DR Genevisible; Q9SVS8; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic 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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..349
FT /note="Gibberellin 3-beta-dioxygenase 3"
FT /id="PRO_0000067315"
FT DOMAIN 201..305
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 296
FT /evidence="ECO:0000255"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 286
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 349 AA; 39211 MW; 7A8F92BC4816CFFC CRC64;
MSSVTQLFKN NPVNRDRIIP LDFTNTKTLP DSHVWSKPEP ETTSGPIPVI SLSNPEEHGL
LRQACEEWGV FHITDHGVSH SLLHNVDCQM KRLFSLPMHR KILAVRSPDE STGYGVVRIS
MFYDKLMWSE GFSVMGSSLR RHATLLWPDD HAEFCNVMEE YQKAMDDLSH RLISMLMGSL
GLTHEDLGWL VPDKTGSGTD SIQSFLQLNS YPVCPDPHLA MGLAPHTDSS LLTILYQGNI
PGLEIESPQE EGSRWIGVEP IEGSLVVIMG DLSHIISNGQ FRSTMHRAVV NKTHHRVSAA
YFAGPPKNLQ IGPLTSDKNH PPIYRRLIWE EYLAAKATHF NKALTLFRC
