GAO1D_WHEAT
ID GAO1D_WHEAT Reviewed; 361 AA.
AC O04705;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Gibberellin 20 oxidase 1-D;
DE EC=1.14.11.- {ECO:0000269|PubMed:16160850};
DE AltName: Full=GA 20-oxidase 1-D;
DE AltName: Full=Gibberellin C-20 oxidase 1-D;
DE AltName: Full=Protein Wga20;
DE AltName: Full=TaGA20ox1-D;
DE Short=Ta20ox1D;
GN Name=GA20ox1D; Synonyms=wga20;
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. April Bearded; TISSUE=Leaf;
RA Youssefian S.;
RT "Characterization of a gibberellin 20-oxidase gene from wheat and its
RT expression in trangenic rice.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000269|PubMed:16160850}.
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:0000269|PubMed:16160850};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60773;
CC Evidence={ECO:0000269|PubMed:16160850};
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:0000269|PubMed:16160850};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60797;
CC Evidence={ECO:0000269|PubMed:16160850};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 nM for GA12 {ECO:0000269|PubMed:16160850};
CC KM=59 nM for GA53 {ECO:0000269|PubMed:16160850};
CC KM=367 nM for GA15 {ECO:0000269|PubMed:16160850};
CC KM=3993 nM for GA44 {ECO:0000269|PubMed:16160850};
CC KM=820 nM for GA24 {ECO:0000269|PubMed:16160850};
CC KM=8640 nM for GA19 {ECO:0000269|PubMed:16160850};
CC -!- TISSUE SPECIFICITY: Expressed in nodes and the ear of the elongating
CC 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. GA20OX subfamily. {ECO:0000305}.
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DR EMBL; Y14007; CAA74330.1; -; mRNA.
DR EMBL; AB005555; BAA21480.1; -; mRNA.
DR PIR; T06330; T06330.
DR AlphaFoldDB; O04705; -.
DR SMR; O04705; -.
DR STRING; 4565.Traes_5DL_3E77D28A6.1; -.
DR PRIDE; O04705; -.
DR EnsemblPlants; TraesCAD_scaffold_014185_01G000100.1; TraesCAD_scaffold_014185_01G000100.1; TraesCAD_scaffold_014185_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_009231_01G000100.1; TraesCLE_scaffold_009231_01G000100.1; TraesCLE_scaffold_009231_01G000100.
DR EnsemblPlants; TraesCS5D02G566200.1; TraesCS5D02G566200.1; TraesCS5D02G566200.
DR EnsemblPlants; TraesPAR_scaffold_027089_01G000100.1; TraesPAR_scaffold_027089_01G000100.1; TraesPAR_scaffold_027089_01G000100.
DR EnsemblPlants; TraesROB_scaffold_019857_01G000200.1; TraesROB_scaffold_019857_01G000200.1; TraesROB_scaffold_019857_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_020254_01G000100.1; TraesWEE_scaffold_020254_01G000100.1; TraesWEE_scaffold_020254_01G000100.
DR Gramene; TraesCAD_scaffold_014185_01G000100.1; TraesCAD_scaffold_014185_01G000100.1; TraesCAD_scaffold_014185_01G000100.
DR Gramene; TraesCLE_scaffold_009231_01G000100.1; TraesCLE_scaffold_009231_01G000100.1; TraesCLE_scaffold_009231_01G000100.
DR Gramene; TraesCS5D02G566200.1; TraesCS5D02G566200.1; TraesCS5D02G566200.
DR Gramene; TraesPAR_scaffold_027089_01G000100.1; TraesPAR_scaffold_027089_01G000100.1; TraesPAR_scaffold_027089_01G000100.
DR Gramene; TraesROB_scaffold_019857_01G000200.1; TraesROB_scaffold_019857_01G000200.1; TraesROB_scaffold_019857_01G000200.
DR Gramene; TraesWEE_scaffold_020254_01G000100.1; TraesWEE_scaffold_020254_01G000100.1; TraesWEE_scaffold_020254_01G000100.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_3_1; -.
DR OMA; HIVEDYF; -.
DR BioCyc; MetaCyc:MON-11641; -.
DR SABIO-RK; O04705; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O04705; baseline.
DR Genevisible; O04705; TA.
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 1: Evidence at protein level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..361
FT /note="Gibberellin 20 oxidase 1-D"
FT /id="PRO_0000219520"
FT DOMAIN 199..299
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 290
FT /evidence="ECO:0000255"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 280
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 361 AA; 40293 MW; 86C254B908AE5F9D CRC64;
MVQPVFDAAV LSGRADIPSQ FIWPEGESPT PDAAEELHVP LIDIGGMLSG DPAAAAEVTR
LVGEACERHG FFQVVNHGID AELLADAHRC VDNFFTMPLP EKQRALRHPG ESCGYASSFT
GRFASKLPWK ETLSFRSCPS DPALVVDYIV ATLGEDHRRL GEVYARYCSE MSRLSLEIME
VLGESLGVGR AHYRRFFEGN DSIMRLNYYP PCQRPLETLG TGPHCDPTSL TILHQDNVGG
LQVHTEGRWR SIRPRADAFV VNIGDTFMAL SNGRYKSCLH RAVVNSRVPR KSLAFFLCPE
MDKVVAPPGT LVDAANPRAY PDFTWRSLLD FTQKHYRADM KTLEVFSSWI VQQQQPQPAR
T
