GAOX5_ARATH
ID GAOX5_ARATH Reviewed; 385 AA.
AC Q4PT02; Q9C6Y1; Q9LNY5;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Gibberellin 20 oxidase 5;
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O04705};
DE AltName: Full=GA 20-oxidase 5;
DE AltName: Full=Gibberellin C-20 oxidase 5;
GN Name=GA20OX5; OrderedLocusNames=At1g44090; ORFNames=F9C16.33, T7O23.20;
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 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 [5]
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 3-day-old seedlings and siliques.
CC Detected in dry seeds, roots, old leaves and inflorescences.
CC {ECO:0000269|PubMed:18069939}.
CC -!- INDUCTION: Not controlled by the level of physiologically active
CC gibberellin. {ECO:0000269|PubMed:18069939}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA20OX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79672.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG50546.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC022314; AAF79672.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC074228; AAG50546.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32018.1; -; Genomic_DNA.
DR EMBL; DQ056484; AAY78641.1; -; mRNA.
DR PIR; B96505; B96505.
DR RefSeq; NP_175075.1; NM_103535.2.
DR AlphaFoldDB; Q4PT02; -.
DR SMR; Q4PT02; -.
DR STRING; 3702.AT1G44090.1; -.
DR PaxDb; Q4PT02; -.
DR PRIDE; Q4PT02; -.
DR EnsemblPlants; AT1G44090.1; AT1G44090.1; AT1G44090.
DR GeneID; 841012; -.
DR Gramene; AT1G44090.1; AT1G44090.1; AT1G44090.
DR KEGG; ath:AT1G44090; -.
DR Araport; AT1G44090; -.
DR TAIR; locus:2037159; AT1G44090.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR InParanoid; Q4PT02; -.
DR OMA; ACMAHGT; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q4PT02; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q4PT02; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4PT02; baseline and differential.
DR Genevisible; Q4PT02; 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..385
FT /note="Gibberellin 20 oxidase 5"
FT /id="PRO_0000422354"
FT DOMAIN 224..324
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 315
FT /evidence="ECO:0000255"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 385 AA; 43161 MW; E0F87BDC5714EC2B CRC64;
MCIYASRQTV CPYLTPFKVK RPKSREMNSS DVNFSLLQSQ PNVPAEFFWP EKDVAPSEGD
LDLPIIDLSG FLNGNEAETQ LAAKAVKKAC MAHGTFLVVN HGFKSGLAEK ALEISSLFFG
LSKDEKLRAY RIPGNISGYT AGHSQRFSSN LPWNETLTLA FKKGPPHVVE DFLTSRLGNH
RQEIGQVFQE FCDAMNGLVM DLMELLGISM GLKDRTYYRR FFEDGSGIFR CNYYPPCKQP
EKALGVGPHN DPTAITVLLQ DDVVGLEVFA AGSWQTVRPR PGALVVNVGD TFMALSNGNY
RSCYHRAVVN KEKVRRSLVF FSCPREDKII VPPPELVEGE EASRKYPDFT WAQLQKFTQS
GYRVDNTTLH NFSSWLVSNS DKKST
