Reviewed, UniProtKB/Swiss-Prot Q9XFR9 (G2OX2_ARATH)

Names and origin

Protein names

Recommended name:
    Gibberellin 2-beta-dioxygenase 2
    EC=1.14.11.13
Alternative name(s):
    Gibberellin 2-beta-hydroxylase 2
    Gibberellin 2-oxidase 2
    GA 2-oxidase 2

Gene names

Name:	GA2OX2
Ordered Locus Names:	At1g30040
ORF Names:	T1P2.6

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development. Converts GA9/GA20 to GA51/GA29 and GA4/GA1 to GA34/GA8. Ref.1
Catalytic activity	Gibberellin 1 + 2-oxoglutarate + O2 = 2-beta-hydroxygibberellin 1 + succinate + CO2.
Cofactor	Iron By similarity.
Pathway	Plant hormone biosynthesis; gibberellin biosynthesis.
Tissue specificity	Preferentially expressed in flowers, siliques, and upper stems. Ref.1
Induction	By gibberellin A3 (GA3). Ref.1
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. GA2OX subfamily. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to red light Inferred from expression pattern. Source: TAIR
Molecular function	gibberellin 2-beta-dioxygenase activity Inferred from electronic annotation. Source: EC iron 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: Q9XFR9-1)

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 – 341	341	Gibberellin 2-beta-dioxygenase 2		PRO_0000067306
Regions
	Domain	179 – 283	105	Fe2OG dioxygenase
Sites
	Active site	274	1	Potential
	Metal binding	207	1	Iron By similarity
	Metal binding	209	1	Iron By similarity
	Metal binding	264	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 83125B5324A62F77	FASTA	341	38,457
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of gibberellin 2-oxidases, multifunctional enzymes involved in gibberellin deactivation." Thomas S.G., Phillips A.L., Hedden P. Proc. Natl. Acad. Sci. U.S.A. 96:4698-4703(1999) [PubMed: 10200325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132436 mRNA. Translation: CAB41008.1. AC022455 Genomic DNA. Translation: AAG52050.1. BT002987 mRNA. Translation: AAO22796.1. BT004464 mRNA. Translation: AAO42458.1.
IPI	IPI00538348.
PIR	T52578.
RefSeq	NP_174296.1.
UniGene	At.412
3D structure databases
SMR	Q9XFR9. Positions 30-321.
ModBase	Search...
Genome annotation databases
GeneID	839883.
GenomeReviews	Gene locus AT1G30040 in contig CT485782_GR.
KEGG	ath:AT1G30040.
NMPDR	fig|3702.1.peg.3340.
Organism-specific databases
GeneFarm	3769. 382.
TAIR	At1g30040.
Phylogenomic databases
HOGENOM	HBG590288.
InParanoid	Q9XFR9.
OMA	FRVNHYP.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G30040-MONOMER.
BRENDA	1.14.11.13. 302.
Gene expression databases
ArrayExpress	Q9XFR9.
Genevestigator	Q9XFR9.
Family and domain databases
InterPro	IPR002283. Isopenicillin-N_synthase. IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
PRINTS	PR00682. IPNSYNTHASE.
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G2OX2_ARATH

Accession

Primary (citable) accession number: Q9XFR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)