ID   G2OX3_ARATH             Reviewed;         335 AA.
AC   O64692;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase 3;
DE            EC=1.14.11.13;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase 3;
DE   AltName: Full=Gibberellin 2-oxidase 3;
DE   AltName: Full=GA 2-oxidase 3;
GN   Name=GA2OX3; OrderedLocusNames=At2g34555; ORFNames=T31E10.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=99218343; PubMed=10200325; DOI=10.1073/pnas.96.8.4698;
RA   Thomas S.G., Phillips A.L., Hedden P.;
RT   "Molecular cloning and functional expression of gibberellin 2-
RT   oxidases, multifunctional enzymes involved in gibberellin
RT   deactivation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4698-4703(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
CC   -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of several
CC       biologically active gibberellins, leading to the homeostatic
CC       regulation of their endogenous level. Catabolism of gibberellins
CC       (GAs) plays a central role in plant development. Converts GA9/GA20
CC       to GA51/GA29 and GA4/GA1 to GA34/GA8.
CC   -!- CATALYTIC ACTIVITY: Gibberellin 1 + 2-oxoglutarate + O(2) = 2-
CC       beta-hydroxygibberellin 1 + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA2OX subfamily.
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DR   EMBL; AJ132437; CAB41009.1; -; mRNA.
DR   EMBL; AC004077; AAM14908.1; -; Genomic_DNA.
DR   IPI; IPI00546397; -.
DR   PIR; T52577; T52577.
DR   RefSeq; NP_181002.1; -.
DR   UniGene; At.413; -.
DR   PRIDE; O64692; -.
DR   GeneID; 818019; -.
DR   GenomeReviews; CT485783_GR; AT2G34555.
DR   KEGG; ath:AT2G34555; -.
DR   NMPDR; fig|3702.1.peg.10550; -.
DR   GeneFarm; 3784; 382.
DR   TAIR; At2g34555; -.
DR   BioCyc; MetaCyc:AT2G34555-MON; -.
DR   BRENDA; 1.14.11.13; 302.
DR   ArrayExpress; O64692; -.
DR   GermOnline; AT2G34555; Arabidopsis thaliana.
DR   GO; GO:0045543; F:gibberellin 2-beta-dioxygenase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    335       Gibberellin 2-beta-dioxygenase 3.
FT                                /FTId=PRO_0000067307.
FT   ACT_SITE    269    269       Potential.
FT   METAL       202    202       Iron (By similarity).
FT   METAL       204    204       Iron (By similarity).
FT   METAL       259    259       Iron (By similarity).
SQ   SEQUENCE   335 AA;  38216 MW;  181F6EAA1EE1C331 CRC64;
     MVIVLQPASF DSNLYVNPKC KPRPVLIPVI DLTDSDAKTQ IVKACEEFGF FKVINHGVRP
     DLLTQLEQEA INFFALHHSL KDKAGPPDPF GYGTKRIGPN GDLGWLEYIL LNANLCLESH
     KTTAIFRHTP AIFREAVEEY IKEMKRMSSK FLEMVEEELK IEPKEKLSRL VKVKESDSCL
     RMNHYPEKEE TPVKEEIGFG EHTDPQLISL LRSNDTEGLQ ICVKDGTWVD VTPDHSSFFV
     LVGDTLQVMT NGRFKSVKHR VVTNTKRSRI SMIYFAGPPL SEKIAPLSCL VPKQDDCLYN
     EFTWSQYKLS AYKTKLGDYR LGLFEKRPPF SLSNV
//