GAOX4_ARATH
ID GAOX4_ARATH Reviewed; 376 AA.
AC Q9C955;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Gibberellin 20 oxidase 4;
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O04705};
DE AltName: Full=GA 20-oxidase 4;
DE AltName: Full=Gibberellin C-20 oxidase 4;
GN Name=GA20OX4; OrderedLocusNames=At1g60980; ORFNames=T7P1.12;
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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY 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 [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: Key oxidase enzyme in the biosynthesis of gibberellin that
CC catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively,
CC via a three-step oxidation at C-20 of the GA skeleton. {ECO:0000250}.
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:0000250|UniProtKB:O04705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC Evidence={ECO:0000250|UniProtKB:O04705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + gibberellin A53 + H(+) + 3 O2 = 3 CO2 +
CC gibberellin A20 + 2 H2O + 2 succinate; Xref=Rhea:RHEA:60796,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58526, ChEBI:CHEBI:143954;
CC Evidence={ECO:0000250|UniProtKB:O04705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797;
CC Evidence={ECO:0000250|UniProtKB:O04705};
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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Detected in leaves,
CC inflorescences and siliques, but not in stems and dry seeds.
CC {ECO:0000269|PubMed:18069939}.
CC -!- INDUCTION: Not controlled by the level of physiologically active
CC gibberellin or by auxin. Up-regulated by paclobutrazol.
CC {ECO:0000269|PubMed:16905669, ECO:0000269|PubMed:18069939}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA20OX subfamily. {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; AC018908; AAG51653.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33755.1; -; Genomic_DNA.
DR EMBL; DQ056503; AAY78660.1; -; mRNA.
DR PIR; D96635; D96635.
DR RefSeq; NP_176294.1; NM_104778.1.
DR AlphaFoldDB; Q9C955; -.
DR SMR; Q9C955; -.
DR STRING; 3702.AT1G60980.1; -.
DR PaxDb; Q9C955; -.
DR PRIDE; Q9C955; -.
DR ProteomicsDB; 248478; -.
DR EnsemblPlants; AT1G60980.1; AT1G60980.1; AT1G60980.
DR GeneID; 842389; -.
DR Gramene; AT1G60980.1; AT1G60980.1; AT1G60980.
DR KEGG; ath:AT1G60980; -.
DR Araport; AT1G60980; -.
DR TAIR; locus:2206036; AT1G60980.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q9C955; -.
DR OMA; RIFDSTV; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9C955; -.
DR BioCyc; MetaCyc:AT1G60980-MON; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9C955; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C955; baseline and differential.
DR Genevisible; Q9C955; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0045544; F:gibberellin 20-oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..376
FT /note="Gibberellin 20 oxidase 4"
FT /id="PRO_0000422353"
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"
SQ SEQUENCE 376 AA; 43133 MW; D66E74790A7C68B4 CRC64;
MECIIKLPQR FNKNKSKKNP LRIFDSTVLN HQPDHIPQEF VWPDHEKPSK NVPILQVPVI
DLAGFLSNDP LLVSEAERLV SEAAKKHGFF LVTNHGVDER LLSTAHKLMD TFFKSPNYEK
LKAQRKVGET TGYASSFVGR FKENLPWKET LSFSFSPTEK SENYSQTVKN YISKTMGDGY
KDFGSVYQEY AETMSNLSLK IMELLGMSLG IKREHFREFF EDNESIFRLN YYPKCKQPDL
VLGTGPHCDP TSLTILQQDQ VSGLQVFVDN QWQSIPPIPQ ALVVNIGDTL MALTNGIYKS
CLHRAVVNGE TTRKTLAFFL CPKVDKVVKP PSELEGERAY PDFTWSMFLE FTMKHYRADM
NTLEEFTNWL KNKGSF
