ID   G2OX1_ARATH             Reviewed;         329 AA.
AC   Q8LEA2; Q9XFR8;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=Gibberellin 2-beta-dioxygenase 1;
DE            EC=1.14.11.13;
DE   AltName: Full=Gibberellin 2-beta-hydroxylase 1;
DE   AltName: Full=Gibberellin 2-oxidase 1;
DE   AltName: Full=GA 2-oxidase 1;
GN   Name=GA2OX1; OrderedLocusNames=At1g78440; ORFNames=F3F9.5;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
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=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Preferentially expressed in flowers, siliques,
CC       and upper stems.
CC   -!- INDUCTION: By gibberellin A3 (GA3).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. GA2OX subfamily.
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DR   EMBL; AJ132435; CAB41007.1; -; mRNA.
DR   EMBL; AC013430; AAF71795.1; -; Genomic_DNA.
DR   EMBL; BT002763; AAO22591.1; -; mRNA.
DR   EMBL; AY085539; AAM62763.1; -; mRNA.
DR   IPI; IPI00540332; -.
DR   PIR; T52579; T52579.
DR   RefSeq; NP_177965.1; -.
DR   UniGene; At.19011; -.
DR   GeneID; 844180; -.
DR   GenomeReviews; CT485782_GR; AT1G78440.
DR   KEGG; ath:AT1G78440; -.
DR   NMPDR; fig|3702.1.peg.7394; -.
DR   GeneFarm; 3768; 382.
DR   TAIR; At1g78440; -.
DR   OMA; Q8LEA2; VSMIYFA.
DR   BioCyc; MetaCyc:AT1G78440-MON; -.
DR   BRENDA; 1.14.11.13; 302.
DR   ArrayExpress; Q8LEA2; -.
DR   GermOnline; AT1G78440; 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; IPR002283; Isopenicillin-N_synthase.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
PE   2: Evidence at transcript level;
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    329       Gibberellin 2-beta-dioxygenase 1.
FT                                /FTId=PRO_0000067305.
FT   ACT_SITE    264    264       Potential.
FT   METAL       197    197       Iron (By similarity).
FT   METAL       199    199       Iron (By similarity).
FT   METAL       254    254       Iron (By similarity).
FT   CONFLICT     10     10       I -> V (in Ref. 4; AAM62763).
FT   CONFLICT     80     80       F -> L (in Ref. 4; AAM62763).
FT   CONFLICT    105    105       H -> L (in Ref. 4; AAM62763).
FT   CONFLICT    139    139       F -> C (in Ref. 4; AAM62763).
SQ   SEQUENCE   329 AA;  36732 MW;  BBD6B0190C12D37C CRC64;
     MAVLSKPVAI PKSGFSLIPV IDMSDPESKH ALVKACEDFG FFKVINHGVS AELVSVLEHE
     TVDFFSLPKS EKTQVAGYPF GYGNSKIGRN GDVGWVEYLL MNANHDSGSG PLFPSLLKSP
     GTFRNALEEY TTSVRKMTFD VLEKITDGLG IKPRNTLSKL VSDQNTDSIL RLNHYPPCPL
     SNKKTNGGKN VIGFGEHTDP QIISVLRSNN TSGLQINLND GSWISVPPDH TSFFFNVGDS
     LQVMTNGRFK SVRHRVLANC KKSRVSMIYF AGPSLTQRIA PLTCLIDNED ERLYEEFTWS
     EYKNSTYNSR LSDNRLQQFE RKTIKNLLN
//