Reviewed,
UniProtKB/Swiss-Prot P29147 (BDH_RAT)
Last modified
November 3, 2009.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: D-beta-hydroxybutyrate dehydrogenase, mitochondrial Short name=BDH EC=1.1.1.30 Alternative name(s): 3-hydroxybutyrate dehydrogenase | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 343 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH. |
| Enzyme regulation | Requires phosphatidylcholine as an allosteric activator for enzymatic activity By similarity. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Allosteric enzyme Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-hydroxybutyrate dehydrogenase activity Ref.1 Traceable author statement. Source: RGD 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 – 46 | 46 | Mitochondrion | ||||||
| Chain | 47 – 343 | 297 | D-beta-hydroxybutyrate dehydrogenase, mitochondrial | PRO_0000031962 | |||||
Regions | |||||||||
| Nucleotide binding | 59 – 83 | 25 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 208 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 195 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 132 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 275 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 90 – 91 | 2 | DK → EQ in AAB59684. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Primary structure of rat liver D-beta-hydroxybutyrate dehydrogenase from cDNA and protein analyses: a short-chain alcohol dehydrogenase." Churchill P., Hempel J., Romovacek H., Zhang W.W., Churchill S., Brennan M. Biochemistry 31:3793-3799(1992) [PubMed: 1567834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Sprague-Dawley. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M89902 mRNA. Translation: AAB59684.1. Different initiation. BC085916 mRNA. Translation: AAH85916.1. Different initiation. | |
| IPI | IPI00480620. |
| PIR | A42345. |
| RefSeq | NP_446447.2. |
| UniGene | Rn.36635 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FDS based on UniProtKB P14061. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P29147. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000002366; ENSRNOP00000002366; ENSRNOG00000001736; Rattus norvegicus. [Genome view] |
| GeneID | 117099. |
| KEGG | rno:117099. |
| NMPDR | fig|10116.3.peg.7406. |
| UCSC | BC085916. rat. |
Organism-specific databases | |
| CTD | 117099. |
| RGD | 620131. Bdh1. |
Phylogenomic databases | |
| HOVERGEN | P29147. |
| OMA | SVTECIV. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.30. 248. |
Gene expression databases | |
| ArrayExpress | P29147. |
| Genevestigator | P29147. |
| GermOnline | ENSRNOG00000001736. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 619980. |
Entry information
| Entry name | BDH_RAT | ||||||||
| Accession | Primary (citable) accession number: P29147 Secondary accession number(s): Q5U2Q2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


