GAOX1_ARATH
ID GAOX1_ARATH Reviewed; 377 AA.
AC Q39110; Q38844; Q9FYN4; Q9FYN5; Q9STJ5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Gibberellin 20 oxidase 1 {ECO:0000305|PubMed:7630935};
DE EC=1.14.11.- {ECO:0000269|PubMed:7630935};
DE AltName: Full=GA 20-oxidase 1 {ECO:0000305|PubMed:7630935};
DE Short=AtGA20ox1;
DE AltName: Full=Gibberellin C-20 oxidase 1;
GN Name=GA20OX1; Synonyms=20ox1, At2301, GA5; OrderedLocusNames=At4g25420;
GN ORFNames=T30C3.90;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND VARIANT LYS-310.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower bud, and Stem;
RX PubMed=7630935; DOI=10.1104/pp.108.3.1049;
RA Phillips A.L., Ward D.A., Uknes S., Appleford N.E.J., Lange T.,
RA Huttly A.K., Gaskin P., Graebe J.E., Hedden P.;
RT "Isolation and expression of three gibberellin 20-oxidase cDNA clones from
RT Arabidopsis.";
RL Plant Physiol. 108:1049-1057(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-310 AND GA5
RP 272-TRP--ILE-377 DEL, AND INDUCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=7604047; DOI=10.1073/pnas.92.14.6640;
RA Xu Y.-L., Li L., Wu K., Peeters A.J.M., Gage D.A., Zeevaart J.A.D.;
RT "The GA5 locus of Arabidopsis thaliana encodes a multifunctional
RT gibberellin 20-oxidase: molecular cloning and functional expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6640-6644(1995).
RN [3]
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 [4]
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 [5]
RP INDUCTION BY COLD.
RX PubMed=14729916; DOI=10.1105/tpc.018143;
RA Yamauchi Y., Ogawa M., Kuwahara A., Hanada A., Kamiya Y., Yamaguchi S.;
RT "Activation of gibberellin biosynthesis and response pathways by low
RT temperature during imbibition of Arabidopsis thaliana seeds.";
RL Plant Cell 16:367-378(2004).
RN [6]
RP INDUCTION BY LIGHT.
RX PubMed=15923331; DOI=10.1104/pp.104.059055;
RA Hisamatsu T., King R.W., Helliwell C.A., Koshioka M.;
RT "The involvement of gibberellin 20-oxidase genes in phytochrome-regulated
RT petiole elongation of Arabidopsis.";
RL Plant Physiol. 138:1106-1116(2005).
RN [7]
RP INDUCTION BY AUXIN AND PACLOBUTRAZOL.
RX PubMed=16905669; DOI=10.1104/pp.106.084871;
RA Frigerio M., Alabadi D., Perez-Gomez J., Garcia-Carcel L., Phillips A.L.,
RA Hedden P., Blazquez M.A.;
RT "Transcriptional regulation of gibberellin metabolism genes by auxin
RT signaling in Arabidopsis.";
RL Plant Physiol. 142:553-563(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP GIBBERELLIN.
RC STRAIN=cv. Columbia;
RX PubMed=18069939; DOI=10.1111/j.1365-313x.2007.03356.x;
RA Rieu I., Ruiz-Rivero O., Fernandez-Garcia N., Griffiths J., Powers S.J.,
RA Gong F., Linhartova T., Eriksson S., Nilsson O., Thomas S.G.,
RA Phillips A.L., Hedden P.;
RT "The gibberellin biosynthetic genes AtGA20ox1 and AtGA20ox2 act, partially
RT redundantly, to promote growth and development throughout the Arabidopsis
RT life cycle.";
RL Plant J. 53:488-504(2008).
RN [9]
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: Key oxidase enzyme in the biosynthesis of gibberellin that
CC catalyzes the conversion of GA12 to GA9, via a three-step oxidation at
CC C-20 of the GA skeleton. GA53 is less effectively oxidized than GA12
CC and is only oxidized one step to GA44 (PubMed:7630935). Involved in the
CC promotion of the floral transition, fertility and silique elongation,
CC but plays only a minor role in elongation of seedling organs. Acts
CC redundantly with GA20OX2 (PubMed:18069939).
CC {ECO:0000269|PubMed:18069939, ECO:0000269|PubMed:7630935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + gibberellin A12 + H(+) + 3 O2 = 3 CO2 +
CC gibberellin A9 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60772,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58627, ChEBI:CHEBI:73255;
CC Evidence={ECO:0000269|PubMed:7630935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC Evidence={ECO:0000269|PubMed:7630935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A12 + O2 = CO2 + gibberellin A15
CC + succinate; Xref=Rhea:RHEA:60776, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58627, ChEBI:CHEBI:143956;
CC Evidence={ECO:0000269|PubMed:7630935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60777;
CC Evidence={ECO:0000269|PubMed:7630935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A15 + O2 = CO2 + gibberellin A24
CC + H2O + succinate; Xref=Rhea:RHEA:60780, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:143956, ChEBI:CHEBI:143957;
CC Evidence={ECO:0000269|PubMed:7630935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60781;
CC Evidence={ECO:0000269|PubMed:7630935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A53 + O2 = CO2 + gibberellin A44
CC + succinate; Xref=Rhea:RHEA:60800, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:143954, ChEBI:CHEBI:143955;
CC Evidence={ECO:0000269|PubMed:7630935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60801;
CC Evidence={ECO:0000269|PubMed:7630935};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and inflorescence
CC tissues. Detected in seeds, roots, leaves and siliques.
CC {ECO:0000269|PubMed:18069939, ECO:0000269|PubMed:7630935}.
CC -!- INDUCTION: Circadian-regulation. Up-regulated by auxin, paclobutrazol
CC and cold treatment. Negatively controlled by the level of
CC physiologically active gibberellin. {ECO:0000269|PubMed:14729916,
CC ECO:0000269|PubMed:15923331, ECO:0000269|PubMed:16905669,
CC ECO:0000269|PubMed:18069939, ECO:0000269|PubMed:7604047}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf. {ECO:0000269|PubMed:18069939}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA20OX subfamily. {ECO:0000305}.
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DR EMBL; X83379; CAA58293.1; -; mRNA.
DR EMBL; U20872; AAC39313.2; -; Genomic_DNA.
DR EMBL; U20873; AAC39314.2; -; Genomic_DNA.
DR EMBL; U20901; AAA76864.2; -; Genomic_DNA.
DR EMBL; AL079350; CAB45519.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81353.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85055.1; -; Genomic_DNA.
DR PIR; T10222; T10222.
DR RefSeq; NP_194272.1; NM_118674.5.
DR AlphaFoldDB; Q39110; -.
DR SMR; Q39110; -.
DR STRING; 3702.AT4G25420.1; -.
DR PaxDb; Q39110; -.
DR PRIDE; Q39110; -.
DR ProteomicsDB; 230474; -.
DR EnsemblPlants; AT4G25420.1; AT4G25420.1; AT4G25420.
DR GeneID; 828645; -.
DR Gramene; AT4G25420.1; AT4G25420.1; AT4G25420.
DR KEGG; ath:AT4G25420; -.
DR Araport; AT4G25420; -.
DR TAIR; locus:2005511; AT4G25420.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q39110; -.
DR OMA; HIVEDYF; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q39110; -.
DR BioCyc; ARA:AT4G25420-MON; -.
DR BioCyc; MetaCyc:AT4G25420-MON; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q39110; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39110; baseline and differential.
DR Genevisible; Q39110; AT.
DR GO; GO:0005737; C:cytoplasm; TAS:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0103055; F:gibberelli A15, 2-oxoglutarate:oxygen oxidoreductase activity; IEA:RHEA.
DR GO; GO:0045544; F:gibberellin 20-oxidase activity; IDA:TAIR.
DR GO; GO:0103054; F:gibberellin A12, 2-oxoglutarate:oxygen oxidoreductase activity (gibberellin A15-forming); IEA:RHEA.
DR GO; GO:0103056; F:gibberellin A53, 2-oxoglutarate:oxygen oxidoreductase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IBA:GO_Central.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR GO; GO:0048575; P:short-day photoperiodism, flowering; IEP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; 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 Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..377
FT /note="Gibberellin 20 oxidase 1"
FT /id="PRO_0000219514"
FT DOMAIN 222..322
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 313
FT /evidence="ECO:0000255"
FT BINDING 247
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VARIANT 272..377
FT /note="Missing (in strain: cv. Landsberg erecta; allele
FT ga5; semidwarfing)"
FT /evidence="ECO:0000269|PubMed:7604047"
FT VARIANT 310
FT /note="E -> K (in strain: cv Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:7604047,
FT ECO:0000269|PubMed:7630935"
FT CONFLICT 7
FT /note="T -> R (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="N -> D (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..41
FT /note="IP -> MA (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> H (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..56
FT /note="INV -> TLQ (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="I -> M (in Ref. 2; AAA76864/AAC39313)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="SE -> RM (in Ref. 2; AAC39314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 43224 MW; 35F4EAD40AE67E7F CRC64;
MAVSFVTTSP EEEDKPKLGL GNIQTPLIFN PSMLNLQANI PNQFIWPDDE KPSINVLELD
VPLIDLQNLL SDPSSTLDAS RLISEACKKH GFFLVVNHGI SEELISDAHE YTSRFFDMPL
SEKQRVLRKS GESVGYASSF TGRFSTKLPW KETLSFRFCD DMSRSKSVQD YFCDALGHGF
QPFGKVYQEY CEAMSSLSLK IMELLGLSLG VKRDYFREFF EENDSIMRLN YYPPCIKPDL
TLGTGPHCDP TSLTILHQDH VNGLQVFVEN QWRSIRPNPK AFVVNIGDTF MALSNDRYKS
CLHRAVVNSE SERKSLAFFL CPKKDRVVTP PRELLDSITS RRYPDFTWSM FLEFTQKHYR
ADMNTLQAFS DWLTKPI
