Reviewed,
UniProtKB/Swiss-Prot Q05963 (FL3H_CALCH)
Last modified
January 19, 2010.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Naringenin,2-oxoglutarate 3-dioxygenase EC=1.14.11.9 Alternative name(s): Flavanone-3-hydroxylase Short name=F3H FHT | ||
| Gene names |
| ||
| Organism | Callistephus chinensis (China aster) | ||
| Taxonomic identifier | 13379 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Astereae › Callistephus |
Protein attributes
| Sequence length | 356 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the 3-beta-hydroxylation of 2S-flavanones to 2R,3R-dihydroflavonols which are intermediates in the biosynthesis of flavonols, anthocyanidins, catechins and proanthocyanidins in plants. |
| Catalytic activity | A flavanone + 2-oxoglutarate + O2 = a dihydroflavonol + succinate + CO2. |
| Cofactor | Iron. Ascorbate. |
| Pathway | |
| Sequence similarities | Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Flavonoid biosynthesis |
| Ligand | Iron Metal-binding Vitamin C |
| Molecular function | Dioxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | flavonoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW naringenin 3-dioxygenase activityInferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred 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 – 356 | 356 | Naringenin,2-oxoglutarate 3-dioxygenase | PRO_0000067284 | |||||
Regions | |||||||||
| Domain | 188 – 292 | 105 | Fe2OG dioxygenase | ||||||
Sites | |||||||||
| Metal binding | 73 | 1 | Iron Potential | ||||||
| Metal binding | 215 | 1 | Iron Potential | ||||||
| Metal binding | 217 | 1 | Iron Potential | ||||||
| Metal binding | 273 | 1 | Iron Potential | ||||||
Sequences
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References
| [1] | "Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues." Britsch L., Dedio J., Saedler H., Forkmann G. Eur. J. Biochem. 217:745-754(1993) [PubMed: 8223617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Flower bud. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X72593 mRNA. Translation: CAA51191.1. |
| PIR | S32147. S38336. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.14.11.9. 275959. |
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 | FL3H_CALCH | ||||||||
| Accession | Primary (citable) accession number: Q05963 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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