G2OX1_PEA
ID G2OX1_PEA Reviewed; 327 AA.
AC Q9SQ80; Q9SQ81; Q9SQJ0; Q9XHM4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Gibberellin 2-beta-dioxygenase 1;
DE EC=1.14.11.13;
DE AltName: Full=GA 2-oxidase 1;
DE AltName: Full=Gibberellin 2-beta-hydroxylase 1;
DE AltName: Full=Gibberellin 2-oxidase 1;
DE AltName: Full=Protein SLENDER;
GN Name=GA2OX1; Synonyms=SLN;
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, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Alaska; TISSUE=Seed;
RX PubMed=10557225; DOI=10.1104/pp.121.3.775;
RA Martin D.N., Proebsting W.M., Hedden P.;
RT "The SLENDER gene of pea encodes a gibberellin 2-oxidase.";
RL Plant Physiol. 121:775-781(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-327, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Torsdag; TISSUE=Seed;
RX PubMed=10417727; DOI=10.1046/j.1365-313x.1999.00501.x;
RA Lester D.R., Ross J.J., Smith J.J., Elliott R.C., Reid J.B.;
RT "Gibberellin 2-oxidation and the SLN gene of Pisum sativum.";
RL Plant J. 19:65-73(1999).
RN [3]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16181493; DOI=10.1186/1471-2229-5-19;
RA Lester D.R., Phillips A., Hedden P., Andersson I.;
RT "Purification and kinetic studies of recombinant gibberellin
RT dioxygenases.";
RL BMC Plant Biol. 5:19-19(2005).
CC -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of several biologically
CC active gibberellins, leading to the homeostatic regulation of their
CC endogenous level. Catabolism of gibberellins (GAs) plays a central role
CC in plant development. Converts GA9/GA20 to GA51/GA29 and GA4/GA1 to
CC GA34/GA8. {ECO:0000269|PubMed:10417727, ECO:0000269|PubMed:10557225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + gibberellin A1 + O2 = CO2 + gibberellin A8 +
CC succinate; Xref=Rhea:RHEA:15005, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58524, ChEBI:CHEBI:58594; EC=1.14.11.13;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.024 uM for GA20 {ECO:0000269|PubMed:16181493};
CC Vmax=4.4 pmol/sec/mg enzyme {ECO:0000269|PubMed:16181493};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots, flowers, young
CC fruits and seeds. {ECO:0000269|PubMed:10417727,
CC ECO:0000269|PubMed:10557225}.
CC -!- DISRUPTION PHENOTYPE: Plants display to the slender phenotype,
CC characterized by large amounts of GA20 that cannot be degraded, and is
CC metabolized to excess GA1 on germination, producing plants with a
CC characteristic slender or hyperelongated phenotype.
CC {ECO:0000269|PubMed:10557225}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. GA2OX subfamily. {ECO:0000305}.
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; AF056935; AAF08609.1; -; mRNA.
DR EMBL; AF101382; AAF13734.1; ALT_SEQ; mRNA.
DR EMBL; AF101383; AAF13735.1; -; Genomic_DNA.
DR EMBL; AF100955; AAD45425.1; -; mRNA.
DR AlphaFoldDB; Q9SQ80; -.
DR SMR; Q9SQ80; -.
DR BioCyc; MetaCyc:MON-11639; -.
DR BRENDA; 1.14.11.13; 4872.
DR SABIO-RK; Q9SQ80; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0052634; F:C-19 gibberellin 2-beta-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..327
FT /note="Gibberellin 2-beta-dioxygenase 1"
FT /id="PRO_0000067311"
FT DOMAIN 171..276
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 267
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 116
FT /note="D -> E (in Ref. 1; AAF13734 and 2; AAD45425)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> H (in Ref. 1; AAF08609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36811 MW; 2728A3B5C871CFB2 CRC64;
MVLLSKPTSE QYTYVRNNMP ITFSSSIPLV DLSKPDAKTL IVKACEDFGF FKVINHGIPL
DAISQLESEA FKFFSLPQTE KEKAGPANPF GYGNKRIGLN GDIGWIEYLL LTTNQDHNFS
LYGEDIDKFR GLLKDYKCAM RNMACEILDL MAEGLKIQPK NVFSKLVMDK QSDCLFRVNH
YPACPELAIN GENLIGFGEH TDPQIISILR SNNTSGFQIS LRDGSWISVP PDHSSFFINV
GDSLQVMTNG RFKSVRHRVL ANGIDPRLSM IYFCGPPLSE KIAPLPSLMK GKESLYKEFT
WFEYKSSTYG SRLADNRLGN YERIAAT
