G3O22_WHEAT
ID G3O22_WHEAT Reviewed; 370 AA.
AC Q3I410;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Gibberellin 3-beta-dioxygenase 2-2;
DE EC=1.14.11.15;
DE AltName: Full=Gibberellin 3 beta-hydroxylase 2-2;
DE AltName: Full=Gibberellin 3-oxidase 2-2;
GN Name=GA3ox2-2;
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], AND FUNCTION.
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. {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 -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA3OX subfamily. {ECO:0000305}.
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DR EMBL; DQ118251; AAZ94378.1; -; mRNA.
DR AlphaFoldDB; Q3I410; -.
DR SMR; Q3I410; -.
DR EnsemblPlants; TraesCAD_scaffold_009178_01G000100.1; TraesCAD_scaffold_009178_01G000100.1; TraesCAD_scaffold_009178_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_007974_01G000100.1; TraesCLE_scaffold_007974_01G000100.1; TraesCLE_scaffold_007974_01G000100.
DR EnsemblPlants; TraesCS3D02G124500.1; TraesCS3D02G124500.1; TraesCS3D02G124500.
DR EnsemblPlants; TraesPAR_scaffold_143758_01G000100.1; TraesPAR_scaffold_143758_01G000100.1; TraesPAR_scaffold_143758_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_013020_01G000100.1; TraesWEE_scaffold_013020_01G000100.1; TraesWEE_scaffold_013020_01G000100.
DR Gramene; TraesCAD_scaffold_009178_01G000100.1; TraesCAD_scaffold_009178_01G000100.1; TraesCAD_scaffold_009178_01G000100.
DR Gramene; TraesCLE_scaffold_007974_01G000100.1; TraesCLE_scaffold_007974_01G000100.1; TraesCLE_scaffold_007974_01G000100.
DR Gramene; TraesCS3D02G124500.1; TraesCS3D02G124500.1; TraesCS3D02G124500.
DR Gramene; TraesPAR_scaffold_143758_01G000100.1; TraesPAR_scaffold_143758_01G000100.1; TraesPAR_scaffold_143758_01G000100.
DR Gramene; TraesWEE_scaffold_013020_01G000100.1; TraesWEE_scaffold_013020_01G000100.1; TraesWEE_scaffold_013020_01G000100.
DR OMA; AITWSEY; -.
DR BioCyc; MetaCyc:MON-11645; -.
DR BRENDA; 1.14.11.15; 6500.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q3I410; 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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..370
FT /note="Gibberellin 3-beta-dioxygenase 2-2"
FT /id="PRO_0000067318"
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; 40355 MW; D8AFF744794CC81E CRC64;
MPTPAHLSKD PRYFDFRAAR RVPETHAWPG LHDHPVVDGS GAGGGPDAVP VVDMRDPCAA
EAVALAAQDW GAFLLEGHGV PLELLARVEA AIAGMFALPA SEKMRAVRRP GDSCGYGSPP
ISSFFSKCMW SEGYTFSPAN LRSDLRKLWP KAGHDYRHFC AVMEEFHREM RALADKLLEL
FLVALGLTGE QVAAVESEQK IAETMTATMH LNWYPKCPDP KRALGLIAHT DSGFFTFVLQ
SLVPGLQLFR HGPDRWVTVP AVPGAMVVNV GDLFQILTNG RFHSVYHRAV VNRDSDRISL
GYFLGPPAHV KVAPLREALA GTPAAYRAVT WPEYMGVRKK AFTTGASALK MVAISTDNDA
ANHTDDLISS
