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UniProtKB/Swiss-Prot entry O49561


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

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Entry information
Entry name G2OX8_ARATH
Primary accession number O49561
Secondary accession numbers None
Integrated into Swiss-Prot on December 20, 2005
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 45)
Name and origin of the protein
Protein name Gibberellin 2-beta-dioxygenase 8
Synonyms EC 1.14.11.13
Gibberellin 2-beta-hydroxylase 8
Gibberellin 2-oxidase 8
GA 2-oxidase 8
Gene name
Name: GA2OX7
OrderedLocusNames: At4g21200
ORFNames: F7J7.140
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
FUNCTION, AND CHARACTERIZATION.
DOI=10.1105/tpc.005975; PubMed=12509528 [NCBI, ExPASy, EBI, Israel, Japan]
Schomburg F.M., Bizzell C.M., Lee D.J., Zeevaart J.A.D., Amasino R.M.;
"Overexpression of a novel class of gibberellin 2-oxidases decreases gibberellin levels and creates dwarf plants.";
Plant Cell 15:151-163(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
AL021960; CAA17539.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161554; CAB79120.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04951; T04951.
3D structure databases
ModBase O49561.
Organism-specific databases
TAIR At4g21200; -.
Gene expression databases
ArrayExpress O49561; -.
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 UniProtKB-KW).
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.
Graphical view of domain structure.
Pfam PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G21200.
NMPDR fig|3702.1.peg.19957; -.
Other
ProtoNet O49561.
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   293  293     Gibberellin 2-beta-dioxygenase 8. PRO_0000067309
ACT_SITE   236   236        Potential. 
METAL   170   170        Iron (By similarity). 
METAL   172   172        Iron (By similarity). 
METAL   226   226        Iron (By similarity). 
Sequence information
Length: 293 AA [This is the length of the unprocessed precursor] Molecular weight: 34050 Da [This is the MW of the unprocessed precursor] CRC64: 5138093F136DF6F6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPPFNEIYN NLLYNQITKK DNDVSEIPFS FSVTAVVEEV ELPVIDVSRL IDGAEEEREK 

        70         80         90        100        110        120 
CKEAIARASR EWGFFQVINH GISMDVLEKM RQEQIRVFRE PFDKKSNSTM EKFASESEAL 

       130        140        150        160        170        180 
AYMLAEVLAE KSGQNSSFFK ENCVRNTCYL RMNRYPPCPK PSEVYGLMPH TDSDFLTILY 

       190        200        210        220        230        240 
QDQVGGLQLI KDNRWIAVKP NPKALIINIG DLFQAWSNGM YKSVEHRVMT NPKVERFSTA 

       250        260        270        280        290 
YFMCPSYDAV IECSSDRPAY RNFSFREFRQ QVQEDVKKFG FKVGLPRFLN HVY 

O49561 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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