Reviewed,
UniProtKB/Swiss-Prot Q08B39 (HOT_XENLA)
Last modified
June 16, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Hydroxyacid-oxoacid transhydrogenase, mitochondrial Short name=HOT EC=1.1.99.24 Alternative name(s): Alcohol dehydrogenase iron-containing protein 1 | ||
| Gene names |
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| Organism | Xenopus laevis (African clawed frog) | ||
| Taxonomic identifier | 8355 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Protein attributes
| Sequence length | 463 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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 | Mitochondrion By 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 |
| 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 | ? – 463 | Hydroxyacid-oxoacid transhydrogenase, mitochondrial | PRO_0000323000 | |||
Sequences
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References
| [1] | NIH - Xenopus Gene Collection (XGC) project Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo. |
Cross-references
Sequence databases | |
|---|---|
| BC124888 mRNA. Translation: AAI24889.1. | |
| RefSeq | NP_001121274.1. |
| UniGene | Xl.15864 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100158357. |
| KEGG | xla:100158357. |
Organism-specific databases | |
| Xenbase | XB-FEAT-966428. adhfe1. |
Phylogenomic databases | |
| HOVERGEN | Q08B39. |
Enzyme and pathway databases | |
| BRENDA | 1.1.99.24. 648. |
Family and domain databases | |
| InterPro | IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [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_XENLA | ||||||||
| Accession | Primary (citable) accession number: Q08B39 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||

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