Q3T046 (BDH2_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 50.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 3-hydroxybutyrate dehydrogenase type 2 EC=1.1.1.- EC=1.1.1.30 Alternative name(s): Dehydrogenase/reductase SDR family member 6 R-beta-hydroxybutyrate dehydrogenase | ||||
| 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 | 245 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase By similarity. |
| Catalytic activity | (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH. |
| Pathway | Siderophore biosynthesis. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | heme metabolic process Inferred from sequence or structural similarity. Source: UniProtKB iron ion homeostasisInferred from sequence or structural similarity. Source: UniProtKB siderophore biosynthetic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-hydroxybutyrate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptorInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 245 | 245 | 3-hydroxybutyrate dehydrogenase type 2 | PRO_0000247551 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 37 | 28 | NAD By similarity | ||||||
| Nucleotide binding | 180 – 184 | 5 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 147 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 58 | 1 | NAD By similarity | ||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||
| Binding site | 151 | 1 | NAD By similarity | ||||||
| Binding site | 188 | 1 | Substrate By similarity | ||||||
| Binding site | 205 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 48 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 132 | 1 | Phosphoserine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC102567 mRNA. Translation: AAI02568.1. |
| IPI | IPI00694312. |
| RefSeq | NP_001029660.1. NM_001034488.1. |
| UniGene | Bt.1792. |
3D structure databases | |
| ProteinModelPortal | Q3T046. |
| SMR | Q3T046. Positions 1-245. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3T046. |
Proteomic databases | |
| PRIDE | Q3T046. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 515321. |
| KEGG | bta:515321. |
Organism-specific databases | |
| CTD | 56898. |
Phylogenomic databases | |
| eggNOG | maNOG04096. |
| GeneTree | ENSGT00600000084182. |
| HOVERGEN | HBG002145. |
| PhylomeDB | Q3T046. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00019. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BDH2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3T046 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with