G3OX4_ARATH
ID G3OX4_ARATH Reviewed; 355 AA.
AC Q9C971; Q1KS84;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 4 {ECO:0000303|PubMed:16181493, ECO:0000303|PubMed:21056641};
DE EC=1.14.11.15 {ECO:0000269|PubMed:16181493};
DE AltName: Full=GA 3-oxidase 4 {ECO:0000303|PubMed:16181493, ECO:0000303|PubMed:21056641};
DE Short=AtGA3ox4 {ECO:0000303|PubMed:16181493, ECO:0000303|PubMed:21056641};
DE AltName: Full=Gibberellin 3 beta-hydroxylase 4 {ECO:0000303|PubMed:16181493, ECO:0000303|PubMed:21056641};
GN Name=GA3OX4 {ECO:0000303|PubMed:16181493, ECO:0000303|PubMed:21056641};
GN OrderedLocusNames=At1g80330 {ECO:0000312|Araport:AT1G80330};
GN ORFNames=F5I6.8 {ECO:0000312|EMBL:AAG52440.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16181493; DOI=10.1186/1471-2229-5-19;
RA Lester D.R., Phillips A., Hedden P., Andersson I.;
RT "Purification and kinetic studies of recombinant gibberellin
RT dioxygenases.";
RL BMC Plant Biol. 5:19-19(2005).
RN [5]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15927942; DOI=10.1093/pcp/pci141;
RA Kim Y.C., Nakajima M., Nakayama A., Yamaguchi I.;
RT "Contribution of gibberellins to the formation of Arabidopsis seed coat
RT through starch degradation.";
RL Plant Cell Physiol. 46:1317-1325(2005).
RN [6]
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 [7]
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 [8]
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:16181493, 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 Evidence={ECO:0000269|PubMed:16181493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10105;
CC Evidence={ECO:0000269|PubMed:16181493};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q5W726};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.85 uM for GA20 {ECO:0000269|PubMed:16181493};
CC Vmax=52500 pmol/sec/mg enzyme {ECO:0000269|PubMed:16181493};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000269|PubMed:16181493}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques and in seeds, specifically at
CC the rim of the embryo and the outer integument. Also expressed in
CC flowers. Not detected in roots, stems and leaves.
CC {ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:16460513,
CC ECO:0000269|PubMed:17277098}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing siliques 3-13 days after
CC pollination. {ECO:0000269|PubMed:15927942}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but abnormal formation of
CC the seed coat. {ECO:0000269|PubMed:15927942}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE97176.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC018848; AAG52440.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36388.1; -; Genomic_DNA.
DR EMBL; DQ459178; ABE97176.1; ALT_FRAME; mRNA.
DR PIR; H96834; H96834.
DR RefSeq; NP_178149.1; NM_106682.1.
DR AlphaFoldDB; Q9C971; -.
DR SMR; Q9C971; -.
DR STRING; 3702.AT1G80330.1; -.
DR PaxDb; Q9C971; -.
DR PRIDE; Q9C971; -.
DR ProteomicsDB; 230541; -.
DR EnsemblPlants; AT1G80330.1; AT1G80330.1; AT1G80330.
DR GeneID; 844373; -.
DR Gramene; AT1G80330.1; AT1G80330.1; AT1G80330.
DR KEGG; ath:AT1G80330; -.
DR Araport; AT1G80330; -.
DR TAIR; locus:2034195; AT1G80330.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9C971; -.
DR OMA; WGGPAGE; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q9C971; -.
DR BioCyc; ARA:AT1G80330-MON; -.
DR BioCyc; MetaCyc:AT1G80330-MON; -.
DR BRENDA; 1.14.11.15; 399.
DR SABIO-RK; Q9C971; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9C971; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C971; baseline and differential.
DR Genevisible; Q9C971; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IDA:TAIR.
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..355
FT /note="Gibberellin 3-beta-dioxygenase 4"
FT /id="PRO_0000067316"
FT DOMAIN 203..303
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 294
FT /evidence="ECO:0000255"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 355 AA; 39153 MW; 9A0333A2112308C1 CRC64;
MPSLAEEICI GNLGSLQTLP ESFTWKLTAA DSLLRPSSAV SFDAVEESIP VIDLSNPDVT
TLIGDASKTW GAFQIANHGI SQKLLDDIES LSKTLFDMPS ERKLEAASSD KGVSGYGEPR
ISPFFEKKMW SEGFTIADDS YRNHFNTLWP HDHTKYCGII QEYVDEMEKL ASRLLYCILG
SLGVTVEDIE WAHKLEKSGS KVGRGAIRLN HYPVCPEPER AMGLAAHTDS TILTILHQSN
TGGLQVFREE SGWVTVEPAP GVLVVNIGDL FHILSNGKIP SVVHRAKVNH TRSRISIAYL
WGGPAGDVQI APISKLTGPA EPSLYRSITW KEYLQIKYEV FDKAMDAIRV VNPTN
