Reviewed,
UniProtKB/Swiss-Prot Q7Q547 (HOT_ANOGA)
Last modified
November 25, 2008.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial Short name=HOT EC=1.1.99.24 | ||
| Gene names |
| ||
| Organism | Anopheles gambiae (African malaria mosquito) [Complete proteome] | ||
| Taxonomic identifier | 7165 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles |
Protein attributes
| Sequence length | 464 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG By similarity. |
| Catalytic activity | (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate. 2-oxoglutaric acid + 4-hydroxybutanoic acid = (R)-2-hydroxyglutaric acid + succinic semialdehyde. |
| Subcellular location | MitochondrionBy similarity. |
| Sequence similarities | Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | molecular hydrogen transport Inferred from sequence or structural similarity. Source: UniProtKB oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | hydroxyacid-oxoacid transhydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |
Molecule processing | ||||||
|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | ||||
| Chain | ? – 464 | Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial | PRO_0000323004 | |||
Sequences
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References
| [1] | "The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. Hoffman S.L.Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST. |
Cross-references
Sequence databases | |
|---|---|
| AAAB01008960 Genomic DNA. Translation: EAA10782.3. | |
| RefSeq | XP_316676.3. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1277230. |
| KEGG | aga:AgaP_AGAP006646. |
| VectorBase | AGAP006646. Anopheles gambiae. |
Family and domain databases | |
| InterPro | IPR001670. Fe_AlcDHase. [Graphical view] |
| Pfam | PF00465. Fe-ADH. 1 hit. [Graphical view] |
| PROSITE | PS00913. ADH_IRON_1. False negative. PS00060. ADH_IRON_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HOT_ANOGA | ||||||||
| Accession | Primary (citable) accession number: Q7Q547 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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