O49561 (G2OX8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gibberellin 2-beta-dioxygenase 8
EC=1.14.11.13

Alternative name(s):
GA 2-oxidase 8
Gibberellin 2-beta-hydroxylase 8
Gibberellin 2-oxidase 8

Gene names

Name:	GA2OX7
Ordered Locus Names:	At4g21200
ORF Names:	F7J7.140

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the 2-beta-hydroxylation of gibberellins (GA) precursors, rendering them unable to be converted to active GAs. Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs, like GA1, GA4, GA9 and GA20. Ref.4
Catalytic activity	Gibberellin 1 + 2-oxoglutarate + O2 = 2-beta-hydroxygibberellin 1 + succinate + CO2.
Cofactor	Iron By similarity.
Pathway	Plant hormone biosynthesis; gibberellin biosynthesis.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. GA2OX subfamily. Contains 1 Fe2OG dioxygenase domain.
Sequence caution	The sequence ABK28642.1 differs from that shown. Reason: Erroneous termination at position 339. Translated as stop. The sequence CAA17539.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79120.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	gibberellin metabolic process Inferred from direct assay Ref.4. Source: TAIR
Molecular function	C-20 gibberellin 2-beta-dioxygenase activity Inferred from direct assay Ref.4. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O49561-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Gibberellin 2-beta-dioxygenase 8		PRO_0000067309
Regions
	Domain	191 – 290	100	Fe2OG dioxygenase
Sites
	Active site	281	1	Potential
	Metal binding	215	1	Iron By similarity
	Metal binding	217	1	Iron By similarity
	Metal binding	271	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 8E2536F78FC3786F	FASTA	338	39,086
	10 20 30 40 50 60 MDPPFNEIYN NLLYNQITKK DNDVSEIPFS FSVTAVVEEV ELPVIDVSRL IDGAEEEREK 70 80 90 100 110 120 CKEAIARASR EWGFFQVINH GISMDVLEKM RQEQIRVFRE PFDKKSKSEK FSAGSYRWGT 130 140 150 160 170 180 PSATSIRQLS WSEAFHVPMT DISDNKDFTT LSSTMEKFAS ESEALAYMLA EVLAEKSGQN 190 200 210 220 230 240 SSFFKENCVR NTCYLRMNRY PPCPKPSEVY GLMPHTDSDF LTILYQDQVG GLQLIKDNRW 250 260 270 280 290 300 IAVKPNPKAL IINIGDLFQA WSNGMYKSVE HRVMTNPKVE RFSTAYFMCP SYDAVIECSS 310 320 330 DRPAYRNFSF REFRQQVQED VKKFGFKVGL PRFLNHVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." 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. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations." Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P. Plant Biotechnol. J. 4:317-324(2006) [PubMed: 17147637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Overexpression of a novel class of gibberellin 2-oxidases decreases gibberellin levels and creates dwarf plants." Schomburg F.M., Bizzell C.M., Lee D.J., Zeevaart J.A.D., Amasino R.M. Plant Cell 15:151-163(2003) [PubMed: 12509528] [Abstract] Cited for: FUNCTION, CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL021960 Genomic DNA. Translation: CAA17539.1. Sequence problems. AL161554 Genomic DNA. Translation: CAB79120.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE84420.1. DQ446856 mRNA. Translation: ABE66080.1. DQ653213 mRNA. Translation: ABK28642.1. Sequence problems.
IPI	IPI00852244.
PIR	T04951.
RefSeq	NP_193852.2. NM_118239.2.
UniGene	At.51238.
3D structure databases
ProteinModelPortal	O49561.
SMR	O49561. Positions 11-316.
ModBase	Search...
Proteomic databases
PRIDE	O49561.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G21200.1; AT4G21200.1; AT4G21200.
GeneID	827868.
GenomeReviews	Gene locus AT4G21200 in contig CT486007_GR.
KEGG	ath:AT4G21200.
NMPDR	fig|3702.1.peg.19957.
Organism-specific databases
TAIR	At4g21200.
Phylogenomic databases
GeneTree	EPGT00050000009705.
HOGENOM	HBG592995.
InParanoid	O49561.
PhylomeDB	O49561.
ProtClustDB	CLSN2920296.
Gene expression databases
ArrayExpress	O49561.
Genevestigator	O49561.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G2OX8_ARATH

Accession

Primary (citable) accession number: O49561
Secondary accession number(s): A0MF87, Q1PE62

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	September 22, 2009
Last modified:	December 14, 2011
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program