Reviewed, UniProtKB/Swiss-Prot Q8LEA2 (G2OX1_ARATH)

Names and origin

Protein names

Recommended name:
    Gibberellin 2-beta-dioxygenase 1
    EC=1.14.11.13
Alternative name(s):
    Gibberellin 2-beta-hydroxylase 1
    Gibberellin 2-oxidase 1
    GA 2-oxidase 1

Gene names

Name:	GA2OX1
Ordered Locus Names:	At1g78440
ORF Names:	F3F9.5

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

Ontologies

Keywords
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
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Gibberellin 2-beta-dioxygenase 1		PRO_0000067305
Sites
	Active site	264	1	Potential
	Metal binding	197	1	Iron By similarity
	Metal binding	199	1	Iron By similarity
	Metal binding	254	1	Iron By similarity
Experimental info
	Sequence conflict	10	1	I → V in AAM62763. Ref.4
	Sequence conflict	80	1	F → L in AAM62763. Ref.4
	Sequence conflict	105	1	H → L in AAM62763. Ref.4
	Sequence conflict	139	1	F → C in AAM62763. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8LEA2-1 [UniParc]. Last modified June 21, 2004. Version 2. Checksum: BBD6B0190C12D37C	FASTA	329	36,732
	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

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.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ132435 mRNA. Translation: CAB41007.1. AC013430 Genomic DNA. Translation: AAF71795.1. BT002763 mRNA. Translation: AAO22591.1. AY085539 mRNA. Translation: AAM62763.1.
IPI	IPI00540332.
PIR	T52579.
RefSeq	NP_177965.1.
UniGene	At.19011
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8LEA2.
Genome annotation databases
GeneID	844180.
GenomeReviews	Gene locus AT1G78440 in contig CT485782_GR.
KEGG	ath:AT1G78440.
NMPDR	fig|3702.1.peg.7394.
Organism-specific databases
GeneFarm	3768. 382.
TAIR	At1g78440.
Phylogenomic databases
OMA	VSMIYFA.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G78440-MON.
BRENDA	1.14.11.13. 302.
Gene expression databases
ArrayExpress	Q8LEA2.
Genevestigator	Q8LEA2.
GermOnline	AT1G78440. Arabidopsis thaliana.
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.
ProtoNet	Search...

Entry information

Entry name

G2OX1_ARATH

Accession

Primary (citable) accession number: Q8LEA2
Secondary accession number(s): Q9XFR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	November 3, 2009
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)