GAO1B_WHEAT
ID GAO1B_WHEAT Reviewed; 365 AA.
AC O04706;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Gibberellin 20 oxidase 1-B;
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O04705};
DE AltName: Full=GA 20-oxidase 1-B;
DE AltName: Full=Gibberellin C-20 oxidase 1-B;
DE AltName: Full=TaGA20ox1-B;
DE Short=Ta20ox1B;
GN Name=GA20ox1B;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP 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: 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: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 cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- TISSUE SPECIFICITY: Not detected in nodes and the ear of the elongating
CC stem. {ECO:0000269|PubMed:16160850}.
CC -!- DEVELOPMENTAL STAGE: 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 -!- MISCELLANEOUS: The expression of this protein encoded by the B genome
CC of the hexaploid wheat is much lower than the one of the two homologous
CC proteins encoded by the A and D genomes.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA20OX subfamily. {ECO:0000305}.
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DR EMBL; Y14008; CAA74331.1; -; mRNA.
DR PIR; T06990; T06990.
DR AlphaFoldDB; O04706; -.
DR SMR; O04706; -.
DR PRIDE; O04706; -.
DR EnsemblPlants; TraesCAD_scaffold_006240_01G000100.1; TraesCAD_scaffold_006240_01G000100.1; TraesCAD_scaffold_006240_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_015042_01G000100.1; TraesCLE_scaffold_015042_01G000100.1; TraesCLE_scaffold_015042_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_058547_01G000100.1; TraesPAR_scaffold_058547_01G000100.1; TraesPAR_scaffold_058547_01G000100.
DR EnsemblPlants; TraesROB_scaffold_006683_01G000200.1; TraesROB_scaffold_006683_01G000200.1; TraesROB_scaffold_006683_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_003667_01G000200.1; TraesWEE_scaffold_003667_01G000200.1; TraesWEE_scaffold_003667_01G000200.
DR Gramene; TraesCAD_scaffold_006240_01G000100.1; TraesCAD_scaffold_006240_01G000100.1; TraesCAD_scaffold_006240_01G000100.
DR Gramene; TraesCLE_scaffold_015042_01G000100.1; TraesCLE_scaffold_015042_01G000100.1; TraesCLE_scaffold_015042_01G000100.
DR Gramene; TraesPAR_scaffold_058547_01G000100.1; TraesPAR_scaffold_058547_01G000100.1; TraesPAR_scaffold_058547_01G000100.
DR Gramene; TraesROB_scaffold_006683_01G000200.1; TraesROB_scaffold_006683_01G000200.1; TraesROB_scaffold_006683_01G000200.
DR Gramene; TraesWEE_scaffold_003667_01G000200.1; TraesWEE_scaffold_003667_01G000200.1; TraesWEE_scaffold_003667_01G000200.
DR BioCyc; MetaCyc:MON-11643; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O04706; baseline.
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..365
FT /note="Gibberellin 20 oxidase 1-B"
FT /id="PRO_0000219519"
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 365 AA; 40737 MW; 61742544357E78BD CRC64;
MVQPVFDAAV LSGRADIPSQ FIWPEGESPT PDAAEELHVP LIDIGGMLSG DPRATAEVTR
LVGEACERHG FFQVVNHGID AELLADAHRC VDAFFTMPLP EKQRALRRPG ESCGYASSFT
GRFASKLPWK ETLSFRSCPS DPALVVDYIV ATLGEDHRRL GEVYARYCSE MSRLSLEIME
VLGESLGVGR AHYRRFFEGN DSIMRLNYYP PCQRPMETLG TGPHCDPTSL TILHQDNVGG
LQVHTEGRWR SIRPRADAFV VNIGDTFMAL SNGRYKSCLH RAVVNSKVPR KSLAFFLCPE
MDKVVAPPGT LVDAANPRAY PDFTWRSLLD FTQKHYRADM KTLEVFSSWI VQQQQGQLLP
PLASH
