Reviewed,
UniProtKB/Swiss-Prot P80456 (ADO_RABIT)
Last modified
July 22, 2008.
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: Aldehyde oxidase EC=1.2.3.1 Alternative name(s): Retinal oxidase | ||||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 1334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2). |
| Cofactor | Binds 2 2Fe-2S clusters. FAD. Molybdopterin. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Very high expression in liver and lung. High expression in kidney, pancreas, brain stem and spinal cord. Moderate expression in heart, testis, eye, cerebral cortex and cerebellum. Low expression in stomach and muscle. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | 2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Molecular function | aldehyde oxidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1334 | 1334 | Aldehyde oxidase | |||||
Regions | ||||||||
| Domain | 5 – 92 | 88 | 2Fe-2S ferredoxin-type | |||||
| Domain | 236 – 421 | 186 | FAD-binding PCMH-type | |||||
Sites | ||||||||
| Metal binding | 44 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
| Metal binding | 49 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
| Metal binding | 52 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
Sequences
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References
| [1] | "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli." Huang D.-Y., Furukawa A., Ichikawa Y. Arch. Biochem. Biophys. 364:264-272(1999) [PubMed: 10190983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 857-884; 891-943 AND 1272-1293. Strain: Japanese white. Tissue: Liver. |
| [2] | "Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase." Turner N.A., Doyle W.A., Ventom A.M., Bray R.C. Eur. J. Biochem. 232:646-657(1995) [PubMed: 7556219] [Abstract] Cited for: PROTEIN SEQUENCE OF 203-231 AND 574-597. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| AB009345 mRNA. Translation: BAA81726.1. | |
| RefSeq | NP_001075459.1. |
| UniGene | Ocu.2359 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FO4 based on UniProtKB P80457. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100008601. |
Phylogenomic databases | |
| HOVERGEN | P80456. |
Family and domain databases | |
| InterPro | IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DHase_a/b. IPR016208. Ald_Oxase/xanthine_DHase. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DHase_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DHase_flav_C. IPR016169. CO_DHase_flavot_FAD-bd_sub2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DHase_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view] |
| Gene3D | G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| Pfam | PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000127. Xanthine_DH. 1 hit. |
| ProDom | PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR02969. mam_aldehyde_ox. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view] |
| BLOCKS | Search... |
Other Resources | |
| ProtoNet | Search... |
Entry information
| Entry name | ADO_RABIT | ||||||||
| Accession | Primary (citable) accession number: P80456 Secondary accession number(s): Q9XTA9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


