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UniProtKB/Swiss-Prot entry Q9XFR9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G2OX2_ARATH
Primary accession number Q9XFR9
Secondary accession numbers None
Integrated into Swiss-Prot on June 21, 2004
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name Gibberellin 2-beta-dioxygenase 2
Synonyms EC 1.14.11.13
Gibberellin 2-beta-hydroxylase 2
Gibberellin 2-oxidase 2
GA 2-oxidase 2
Gene name
Name: GA2OX2
OrderedLocusNames: At1g30040
ORFNames: T1P2.6
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.96.8.4698; PubMed=10200325 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas S.G., Phillips A.L., Hedden P.;
"Molecular cloning and functional expression of gibberellin 2-oxidases, multifunctional enzymes involved in gibberellin deactivation.";
Proc. Natl. Acad. Sci. U.S.A. 96:4698-4703(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ132436; CAB41008.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC022455; AAG52050.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002987; AAO22796.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004464; AAO42458.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T52578; T52578.
RefSeq NP_174296.1; -.
UniGene At.412
3D structure databases
ModBase Q9XFR9.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G30040-MON; -.
Organism-specific databases
GeneFarm 3769; 382.
TAIR At1g30040; -.
Gene expression databases
ArrayExpress Q9XFR9; -.
Ontologies
GO
GO:0045543; Molecular function: gibberellin 2-beta-dioxygenase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005123; 2OG-FeII_Oase.
IPR002283; Isopenicillin-N_synthase.
Graphical view of domain structure.
Pfam PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.
PRINTS PR00682; IPNSYNTHASE.
BLOCKS Q9XFR9.
ProtoNet Q9XFR9.
Genome annotation databases
GeneID 839883; -.
GenomeReviews CT485782_GR; AT1G30040.
NMPDR fig|3702.1.peg.3340; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   341  341     Gibberellin 2-beta-dioxygenase 2. PRO_0000067306
ACT_SITE   274   274        Potential. 
METAL   207   207        Iron (By similarity). 
METAL   209   209        Iron (By similarity). 
METAL   264   264        Iron (By similarity). 
Sequence information
Length: 341 AA [This is the length of the unprocessed precursor] Molecular weight: 38457 Da [This is the MW of the unprocessed precursor] CRC64: 83125B5324A62F77 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVLPQPVTL DNHISLIPTY KPVPVLTSHS IPVVNLADPE AKTRIVKACE EFGFFKVVNH 

        70         80         90        100        110        120 
GVRPELMTRL EQEAIGFFGL PQSLKNRAGP PEPYGYGNKR IGPNGDVGWI EYLLLNANPQ 

       130        140        150        160        170        180 
LSSPKTSAVF RQTPQIFRES VEEYMKEIKE VSYKVLEMVA EELGIEPRDT LSKMLRDEKS 

       190        200        210        220        230        240 
DSCLRLNHYP AAEEEAEKMV KVGFGEHTDP QIISVLRSNN TAGLQICVKD GSWVAVPPDH 

       250        260        270        280        290        300 
SSFFINVGDA LQVMTNGRFK SVKHRVLADT RRSRISMIYF GGPPLSQKIA PLPCLVPEQD 

       310        320        330        340 
DWLYKEFTWS QYKSSAYKSK LGDYRLGLFE KQPLLNHKTL V 

Q9XFR9 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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