Reviewed,
UniProtKB/Swiss-Prot P24397 (HY6H_HYONI)
Last modified
January 19, 2010.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Hyoscyamine 6-dioxygenase EC=1.14.11.11 Alternative name(s): Hyoscyamine 6-beta-hydroxylase | ||
| Gene names |
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| Organism | Hyoscyamus niger (Black henbane) | ||
| Taxonomic identifier | 4079 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Hyoscyameae › Hyoscyamus |
Protein attributes
| Sequence length | 344 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | L-hyoscyamine + 2-oxoglutarate + O2 = (6S)-hydroxyhyoscyamine + succinate + CO2. |
| Cofactor | Iron. Ascorbate. |
| Pathway | |
| Subunit structure | Monomer. |
| Tissue specificity | Root. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Iron Metal-binding Vitamin C |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW hyoscyamine (6S)-dioxygenase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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)
Sequences
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References
| [1] | "Molecular cloning of hyoscyamine 6 beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger." Matsuda J., Okabe S., Hashimoto T., Yamada Y. J. Biol. Chem. 266:9460-9464(1991) [PubMed: 2033047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE. Tissue: Root. |
| [2] | "Species-dependent expression of the hyoscyamine 6 beta-hydroxylase gene in the pericycle." Kanegae T., Kajiya H., Amano Y., Hashimoto T., Yamada Y. Plant Physiol. 105:483-490(1994) [PubMed: 8066129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M62719 mRNA. Translation: AAA33387.1. D26583 Genomic DNA. Translation: BAA05630.1. |
| PIR | A40005. |
3D structure databases | |
| SMR | P24397. Positions 9-331. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.14.11.11. 95966. |
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 | HY6H_HYONI | ||||||||
| Accession | Primary (citable) accession number: P24397 | ||||||||
| 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 |

Clusters with


