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UniProtKB/Swiss-Prot entry Q8LEA2


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

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Entry information
Entry name G2OX1_ARATH
Primary accession number Q8LEA2
Secondary accession number Q9XFR8
Integrated into Swiss-Prot on June 21, 2004
Sequence was last modified on June 21, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Gibberellin 2-beta-dioxygenase 1
Synonyms EC 1.14.11.13
Gibberellin 2-beta-hydroxylase 1
Gibberellin 2-oxidase 1
GA 2-oxidase 1
Gene name
Name: GA2OX1
OrderedLocusNames: At1g78440
ORFNames: F3F9.5
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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
AJ132435; CAB41007.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC013430; AAF71795.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002763; AAO22591.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY085539; AAM62763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T52579; T52579.
RefSeq NP_177965.1; -.
UniGene At.19011
3D structure databases
ModBase Q8LEA2.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G78440-MON; -.
Organism-specific databases
GeneFarm 3768; 382.
TAIR At1g78440; -.
Gene expression databases
ArrayExpress Q8LEA2; -.
GermOnline AT1G78440; Arabidopsis thaliana.
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.
Genome annotation databases
GeneID 844180; -.
GenomeReviews CT485782_GR; AT1G78440.
KEGG ath:AT1G78440; -.
NMPDR fig|3702.1.peg.7394; -.
Other
ProtoNet Q8LEA2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   329  329     Gibberellin 2-beta-dioxygenase 1. PRO_0000067305
ACT_SITE   264   264        Potential. 
METAL   197   197        Iron (By similarity). 
METAL   199   199        Iron (By similarity). 
METAL   254   254        Iron (By similarity). 
CONFLICT   10    10        I -> V (in Ref. 4; AAM62763). 
CONFLICT   80    80        F -> L (in Ref. 4; AAM62763). 
CONFLICT   105   105        H -> L (in Ref. 4; AAM62763). 
CONFLICT   139   139        F -> C (in Ref. 4; AAM62763). 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36732 Da [This is the MW of the unprocessed precursor] CRC64: BBD6B0190C12D37C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVLSKPVAI PKSGFSLIPV IDMSDPESKH ALVKACEDFG FFKVINHGVS AELVSVLEHE 

        70         80         90        100        110        120 
TVDFFSLPKS EKTQVAGYPF GYGNSKIGRN GDVGWVEYLL MNANHDSGSG PLFPSLLKSP 

       130        140        150        160        170        180 
GTFRNALEEY TTSVRKMTFD VLEKITDGLG IKPRNTLSKL VSDQNTDSIL RLNHYPPCPL 

       190        200        210        220        230        240 
SNKKTNGGKN VIGFGEHTDP QIISVLRSNN TSGLQINLND GSWISVPPDH TSFFFNVGDS 

       250        260        270        280        290        300 
LQVMTNGRFK SVRHRVLANC KKSRVSMIYF AGPSLTQRIA PLTCLIDNED ERLYEEFTWS 

       310        320 
EYKNSTYNSR LSDNRLQQFE RKTIKNLLN 

Q8LEA2 in FASTA format

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