G3O21_WHEAT
ID G3O21_WHEAT Reviewed; 370 AA.
AC Q3I411;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 2-1;
DE EC=1.14.11.15;
DE AltName: Full=Gibberellin 3 beta-hydroxylase 2-1;
DE AltName: Full=Gibberellin 3-oxidase 2-1;
GN Name=GA3ox2-1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Maris Huntsman; TISSUE=Scutellum;
RX PubMed=16160850; DOI=10.1007/s00425-005-0104-0;
RA Appleford N.E., Evans D.J., Lenton J.R., Gaskin P., Croker S.J.,
RA Devos K.M., Phillips A.L., Hedden P.;
RT "Function and transcript analysis of gibberellin-biosynthetic enzymes in
RT wheat.";
RL Planta 223:568-582(2006).
CC -!- FUNCTION: Converts the inactive gibberellin precursors GA9 and GA20 in
CC the bioactives gibberellins GA4 and GA1. Accepts also GA15, GA44, the
CC 2,3-unsaturated GA5 and 2,3-dihydroGA9 as substrate. No activity with
CC GA12, GA53, GA24, GA19 and GA25. Possesses also 2-beta-hydroxylase,
CC 2,3-desaturase, 2,3-epoxidase and 13-hydroxylase activities.
CC {ECO:0000269|PubMed:16160850}.
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 -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for GA9 {ECO:0000269|PubMed:16160850};
CC KM=2.02 uM for GA20 {ECO:0000269|PubMed:16160850};
CC -!- TISSUE SPECIFICITY: Expressed in internodes, nodes and the ear of the
CC elongating stem. {ECO:0000269|PubMed:16160850}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the embryo and the surrounding
CC maternal tissues, the pericarp and the integuments. Also found in the
CC germinating grain. {ECO:0000269|PubMed:16160850}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
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DR EMBL; DQ118250; AAZ94377.1; -; mRNA.
DR AlphaFoldDB; Q3I411; -.
DR SMR; Q3I411; -.
DR PRIDE; Q3I411; -.
DR EnsemblPlants; TraesCAD_scaffold_086214_01G000100.1; TraesCAD_scaffold_086214_01G000100.1; TraesCAD_scaffold_086214_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_050980_01G000100.1; TraesCLE_scaffold_050980_01G000100.1; TraesCLE_scaffold_050980_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_090669_01G000100.1; TraesPAR_scaffold_090669_01G000100.1; TraesPAR_scaffold_090669_01G000100.
DR EnsemblPlants; TraesROB_scaffold_121309_01G000100.1; TraesROB_scaffold_121309_01G000100.1; TraesROB_scaffold_121309_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_061575_01G000100.1; TraesWEE_scaffold_061575_01G000100.1; TraesWEE_scaffold_061575_01G000100.
DR Gramene; TraesCAD_scaffold_086214_01G000100.1; TraesCAD_scaffold_086214_01G000100.1; TraesCAD_scaffold_086214_01G000100.
DR Gramene; TraesCLE_scaffold_050980_01G000100.1; TraesCLE_scaffold_050980_01G000100.1; TraesCLE_scaffold_050980_01G000100.
DR Gramene; TraesPAR_scaffold_090669_01G000100.1; TraesPAR_scaffold_090669_01G000100.1; TraesPAR_scaffold_090669_01G000100.
DR Gramene; TraesROB_scaffold_121309_01G000100.1; TraesROB_scaffold_121309_01G000100.1; TraesROB_scaffold_121309_01G000100.
DR Gramene; TraesWEE_scaffold_061575_01G000100.1; TraesWEE_scaffold_061575_01G000100.1; TraesWEE_scaffold_061575_01G000100.
DR BioCyc; MetaCyc:MON-11644; -.
DR BRENDA; 1.14.11.15; 6500.
DR SABIO-RK; Q3I411; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q3I411; baseline and differential.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0016707; F:gibberellin 3-beta-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
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..370
FT /note="Gibberellin 3-beta-dioxygenase 2-1"
FT /id="PRO_0000067317"
FT DOMAIN 205..306
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 297
FT /evidence="ECO:0000255"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 370 AA; 40245 MW; 34930E368D91D3DD CRC64;
MPTPSHLSKD PRYFDFRAAR RVPETHAWPG LHDHPVVDGS GAGGGPDAVP VVDMRDPCAA
EAVALAAQDW GAFLLEGHGV PLELLAGVEA AIGGMFALPA SEKMRAVRRP GDSCGYGSPP
ISSFFSKCMW SEGYTFSPAN LRSDLRKLWP KAGHDYRHFC AVMEEFHREM RALADKLLEL
FLVALGLTGE QVAAVESEHK IAETMTATMH LNWYPKCPDP KRALGLIAHT DSGFFTFVLQ
SLVPGLQLFR HGPDRWVTVP AVPGAMVVNV GDLFQILTNG RFHSVYHRAV VNRDSDRISL
GYFLGPPAHV KVAPLREALA GTPAAYRAVT WPEYMGVRKK AFTTGASALK MVAISTDNDA
ANDTDDLISS
