[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTANT SLENDER. STRAIN=cv. Alaska; TISSUE=Seed; DOI=10.1104/pp.121.3.775; PubMed=10557225 [NCBI, ExPASy, EBI, Israel, Japan] Martin D.N., Proebsting W.M., Hedden P.; "The SLENDER gene of pea encodes a gibberellin 2-oxidase."; Plant Physiol. 121:775-781(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 6-327, FUNCTION, AND TISSUE SPECIFICITY. STRAIN=cv. Torsdag; TISSUE=Seed; PubMed=10417727 [NCBI, ExPASy, EBI, Israel, Japan] Lester D.R., Ross J.J., Smith J.J., Elliott R.C., Reid J.B.; "Gibberellin 2-oxidation and the SLN gene of Pisum sativum."; Plant J. 19:65-73(1999).
[3]	CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1186/1471-2229-5-19; PubMed=16181493 [NCBI, ExPASy, EBI, Israel, Japan] Lester D.R., Phillips A., Hedden P., Andersson I.; "Purification and kinetic studies of recombinant gibberellin dioxygenases."; BMC Plant Biol. 5:19-19(2005).

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.
CATALYTIC ACTIVITY: Gibberellin 1 + 2-oxoglutarate + O₂ = 2-beta-hydroxygibberellin 1 + succinate + CO₂.
COFACTOR: Iron (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=0.024 µM for GA20;
V_max=4.4 pmol/sec/mg enzyme;
PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis .
TISSUE SPECIFICITY: Predominantly expressed in roots, flowers, young fruits and seeds.
MISCELLANEOUS: Defects in GA2ox1 lead to the slender phenotype, characterized by large amounts of GA20 that cannot be degraded, and is metabolized to excess GA1 on germination, producing plants with a characteristic slender or hyperelongated phenotype.
SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA2OX subfamily.

Copyright

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Cross-references

Sequence databases

EMBL

AF056935; AAF08609.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF101382; AAF13734.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF101383; AAF13735.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF100955; AAD45425.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9SQ80.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11639; -.

Ontologies

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 InterPro).
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.
IPR002283; Isopenicillin-N_synthase.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

PRINTS

PR00682; IPNSYNTHASE.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 327`	`327`	`Gibberellin 2-beta-dioxygenase 1.`	`PRO_0000067311`
`ACT_SITE`	`267 267`		`Potential.`
`METAL`	`200 200`		`Iron (By similarity).`
`METAL`	`202 202`		`Iron (By similarity).`
`METAL`	`257 257`		`Iron (By similarity).`
`CONFLICT`	`116 116`		`D -> E (in Ref. 1; AAF13734 and 2; AAD45425).`
`CONFLICT`	`127 127`		`D -> H (in Ref. 1; AAF08609).`

Sequence information

Length: 327 AA [This is the length of the unprocessed precursor]

Molecular weight: 36811 Da [This is the MW of the unprocessed precursor]

CRC64: 2728A3B5C871CFB2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLLSKPTSE QYTYVRNNMP ITFSSSIPLV DLSKPDAKTL IVKACEDFGF FKVINHGIPL 

        70         80         90        100        110        120 
DAISQLESEA FKFFSLPQTE KEKAGPANPF GYGNKRIGLN GDIGWIEYLL LTTNQDHNFS 

       130        140        150        160        170        180 
LYGEDIDKFR GLLKDYKCAM RNMACEILDL MAEGLKIQPK NVFSKLVMDK QSDCLFRVNH 

       190        200        210        220        230        240 
YPACPELAIN GENLIGFGEH TDPQIISILR SNNTSGFQIS LRDGSWISVP PDHSSFFINV 

       250        260        270        280        290        300 
GDSLQVMTNG RFKSVRHRVL ANGIDPRLSM IYFCGPPLSE KIAPLPSLMK GKESLYKEFT 

       310        320 
WFEYKSSTYG SRLADNRLGN YERIAAT

Q9SQ80 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools