Reviewed,
UniProtKB/Swiss-Prot O73688 (HMOX_FUGRU)
Last modified
June 16, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heme oxygenase Short name=HO EC=1.14.99.3 | ||
| Gene names |
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| Organism | Fugu rubripes (Japanese pufferfish) (Takifugu rubripes) | ||
| Taxonomic identifier | 31033 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu |
Protein attributes
| Sequence length | 277 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed By similarity. |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | Microsome By similarity. Endoplasmic reticulum By similarity. |
| Sequence similarities | Belongs to the heme oxygenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Microsome |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | heme oxidation Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The pufferfish SLP-1 gene, a new member of the SCL/TAL-1 family of transcription factors." Gottgens B., Gilbert J.G.R., Barton L.M., Aparicio S., Hawker K., Mistry S., Vaudin M., King A., Bentley D., Elgar G., Green A.R. Genomics 48:52-62(1998) [PubMed: 9503016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF022814 Genomic DNA. Translation: AAC41263.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N45 based on UniProtKB P09601. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | O73688. |
Enzyme and pathway databases | |
| BRENDA | 1.14.99.3. 281122. |
Family and domain databases | |
| InterPro | IPR002051. Haem_Oase. IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR018207. Haem_oxygenase_CS. [Graphical view] |
| Gene3D | G3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit. |
| PANTHER | PTHR10720. Haem_Oase. 1 hit. |
| Pfam | PF01126. Heme_oxygenase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000343. Haem_Oase. 1 hit. |
| PRINTS | PR00088. HAEMOXYGNASE. |
| PROSITE | PS00593. HEME_OXYGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMOX_FUGRU | ||||||||
| Accession | Primary (citable) accession number: O73688 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


