G3OX_PEA
ID G3OX_PEA Reviewed; 374 AA.
AC O24648; O22377; O24623; O24627;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 1;
DE EC=1.14.11.15;
DE AltName: Full=GA 3-oxidase 1;
DE AltName: Full=Gibberellin 3 beta-hydroxylase 1;
GN Name=LE;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ALA-229.
RX PubMed=9286112; DOI=10.2307/3870393;
RA Lester D.R., Ross J.J., Davies P.J., Reid J.B.;
RT "Mendel's stem length gene (Le) encodes a gibberellin 3 beta-hydroxylase.";
RL Plant Cell 9:1435-1443(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP MUTAGENESIS OF LEU-89; ALA-229 AND HIS-276, AND DISRUPTION PHENOTYPE.
RX PubMed=9238076; DOI=10.1073/pnas.94.16.8907;
RA Martin D.N., Proebsting W.M., Hedden P.;
RT "Mendel's dwarfing gene: cDNAs from the Le alleles and function of the
RT expressed proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8907-8911(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS OF HIS-276, FUNCTION,
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RA Lester D.R., Mackenzie-Hose A.K., Davies P.J., Ross J.J., Reid J.B.;
RT "The influence of the null le-2 mutation on gibberellin levels in
RT developing pea seeds.";
RL Plant Growth Regul. 27:83-89(1999).
CC -!- FUNCTION: Converts the inactive gibberellin (GA) precursors GA9 and
CC GA20 in the bioactives gibberellins GA4 and GA1. Has a small activity
CC on GA29, producing GA8. Unable to convert GA20 to GA5, GA5 to GA3 or
CC GA12 to GA14. Involved in the production of bioactive GA for vegetative
CC growth and development, but not for the 3-beta-hydroxylation of GA in
CC developing seeds. {ECO:0000269|PubMed:9238076,
CC ECO:0000269|PubMed:9286112, ECO:0000269|Ref.3}.
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:9238076, ECO:0000269|PubMed:9286112,
CC ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for GA9 {ECO:0000269|PubMed:9238076};
CC KM=13 uM for GA20 {ECO:0000269|PubMed:9238076};
CC Vmax=0.29 nmol/min/mg enzyme with GA9 as substrate
CC {ECO:0000269|PubMed:9238076};
CC Vmax=0.10 nmol/min/mg enzyme with GA20 as substrate
CC {ECO:0000269|PubMed:9238076};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in radicles, roots, internodes,
CC cotyledons, leaves and shoots. Barely detected in developing seeds. Not
CC detected in flowers or young fruits. {ECO:0000269|PubMed:9238076,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in germinating seedlings.
CC {ECO:0000269|PubMed:9238076}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. {ECO:0000269|PubMed:9238076}.
CC -!- MISCELLANEOUS: The Le gene controls the stem length trait studied by
CC Gregor Mendel in 1866 (PubMed:9286112 and PubMed:9238076).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On the garden pea - Issue
CC 159 of April 2014;
CC URL="https://web.expasy.org/spotlight/back_issues/159/";
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; U85045; AAB65829.1; -; mRNA.
DR EMBL; AF001219; AAC49792.1; -; mRNA.
DR EMBL; AF010167; AAC49793.1; -; mRNA.
DR EMBL; AF010168; AAC49794.1; -; mRNA.
DR EMBL; U93210; AAC86820.1; -; Genomic_DNA.
DR EMBL; AF007766; AAC96017.1; -; mRNA.
DR EMBL; AF004730; AAC96015.1; -; Genomic_DNA.
DR PIR; T06244; T06244.
DR PIR; T06245; T06245.
DR AlphaFoldDB; O24648; -.
DR SMR; O24648; -.
DR SABIO-RK; O24648; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IDA:UniProtKB.
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.
FT CHAIN 1..374
FT /note="Gibberellin 3-beta-dioxygenase 1"
FT /id="PRO_0000425239"
FT DOMAIN 206..307
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 298
FT /evidence="ECO:0000255"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 298
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 89
FT /note="L->F: Strongly decreased catalytic activity
FT producing a dwarf phenotype; when associated with Y-276."
FT /evidence="ECO:0000269|PubMed:9238076"
FT MUTAGEN 229
FT /note="A->T: In le-1; strongly decreased catalytic activity
FT producing a dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:9238076,
FT ECO:0000269|PubMed:9286112"
FT MUTAGEN 276
FT /note="H->Y: In le-3; strongly decreased catalytic activity
FT producing a dwarf phenotype. Strongly decreased catalytic
FT activity producing a dwarf phenotype; when associated with
FT F-89."
FT /evidence="ECO:0000269|PubMed:9238076, ECO:0000269|Ref.3"
SQ SEQUENCE 374 AA; 41726 MW; B7203F5FB264C9C9 CRC64;
MPSLSEAYRA HPVHVNHKHP DFNSLQELPE SYNWTHLDDH TLIDSNNIMK ESTTTVPVID
LNDPNASKLI GLACKTWGVY QVMNHGIPLS LLEDIQWLGQ TLFSLPSHQK HKATRSPDGV
SGYGIARISS FFPKLMWYEG FTIVGSPLDH FRELWPQDYT RFCDIVVQYD ETMKKLAGTL
MCLMLDSLGI TKEDIKWAGS KAQFEKACAA LQLNSYPSCP DPDHAMGLAP HTDSTFLTIL
SQNDISGLQV NREGSGWITV PPLQGGLVVN VGDLFHILSN GLYPSVLHRV LVNRTRQRFS
VAYLYGPPSN VEICPHAKLI GPTKPPLYRS VTWNEYLGTK AKHFNKALSS VRLCTPINGL
FDVNDSNKNS VQVG
