ID G2OX8_ARATH Reviewed; 293 AA. AC O49561; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 49. DE RecName: Full=Gibberellin 2-beta-dioxygenase 8; DE EC=1.14.11.13; DE AltName: Full=Gibberellin 2-beta-hydroxylase 8; DE AltName: Full=Gibberellin 2-oxidase 8; DE AltName: Full=GA 2-oxidase 8; GN Name=GA2OX7; OrderedLocusNames=At4g21200; ORFNames=F7J7.140; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP FUNCTION, AND CHARACTERIZATION. RX MEDLINE=22397961; PubMed=12509528; DOI=10.1105/tpc.005975; RA Schomburg F.M., Bizzell C.M., Lee D.J., Zeevaart J.A.D., Amasino R.M.; RT "Overexpression of a novel class of gibberellin 2-oxidases decreases RT gibberellin levels and creates dwarf plants."; RL Plant Cell 15:151-163(2003). CC -!- FUNCTION: Catalyzes the 2-beta-hydroxylation of gibberellins (GA) CC precursors, rendering them unable to be converted to active GAs. CC Hydroxylates the C20-GA GA12 and GA53, but is not active on C19- CC GAs, like GA1, GA4, GA9 and GA20. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL021960; CAA17539.1; -; Genomic_DNA. DR EMBL; AL161554; CAB79120.1; -; Genomic_DNA. DR IPI; IPI00852244; -. DR PIR; T04951; T04951. DR GenomeReviews; CT486007_GR; AT4G21200. DR NMPDR; fig|3702.1.peg.19957; -. DR TAIR; At4g21200; -. DR OMA; O49561; WSEAYHI. DR BRENDA; 1.14.11.13; 302. DR ArrayExpress; O49561; -. DR GO; GO:0045543; F:gibberellin 2-beta-dioxygenase activity; IDA:TAIR. 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 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase. FT CHAIN 1 293 Gibberellin 2-beta-dioxygenase 8. FT /FTId=PRO_0000067309. FT ACT_SITE 236 236 Potential. FT METAL 170 170 Iron (By similarity). FT METAL 172 172 Iron (By similarity). FT METAL 226 226 Iron (By similarity). SQ SEQUENCE 293 AA; 34050 MW; 5138093F136DF6F6 CRC64; MDPPFNEIYN NLLYNQITKK DNDVSEIPFS FSVTAVVEEV ELPVIDVSRL IDGAEEEREK CKEAIARASR EWGFFQVINH GISMDVLEKM RQEQIRVFRE PFDKKSNSTM EKFASESEAL AYMLAEVLAE KSGQNSSFFK ENCVRNTCYL RMNRYPPCPK PSEVYGLMPH TDSDFLTILY QDQVGGLQLI KDNRWIAVKP NPKALIINIG DLFQAWSNGM YKSVEHRVMT NPKVERFSTA YFMCPSYDAV IECSSDRPAY RNFSFREFRQ QVQEDVKKFG FKVGLPRFLN HVY //