Reviewed,
UniProtKB/Swiss-Prot A6QP15 (HOT_BOVIN)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 466 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 | ? – 466 | Hydroxyacid-oxoacid transhydrogenase, mitochondrial | PRO_0000322995 | |||
Sequences
| ||||||||||||||||||
References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| BC149097 mRNA. Translation: AAI49098.1. | |
| IPI | IPI00867494. |
| RefSeq | NP_001095357.1. |
| UniGene | Bt.47646 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAG00000004476. Bos taurus. [Contig view] |
| GeneID | 507711. |
| KEGG | bta:507711. |
Enzyme and pathway databases | |
| BRENDA | 1.1.99.24. 251. |
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_BOVIN | ||||||||
| Accession | Primary (citable) accession number: A6QP15 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


