P26298 (LDHD_LACPE) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 67.
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: D-lactate dehydrogenase Short name=D-LDH EC=1.1.1.28 Alternative name(s): D-specific D-2-hydroxyacid dehydrogenase |
| Organism | Lactobacillus pentosus |
| Taxonomic identifier | 1589 [NCBI] |
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | (R)-lactate + NAD+ = pyruvate + NADH. |
| Subunit structure | Homodimer. |
| Miscellaneous | Also active on D-glycerate. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. |
| Caution | Was originally (Ref.1) thought to originate from L.plantarum. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Molecular function | D-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 332 | 332 | D-lactate dehydrogenase | PRO_0000075956 | |||||
Regions | |||||||||
| Nucleotide binding | 155 – 156 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 233 – 235 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 296 – 299 | 4 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 235 | 1 | |||||||
| Active site | 264 | 1 | |||||||
| Active site | 296 | 1 | Proton donor | ||||||
Sequences
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References
| [1] | "D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum." Ohta T., Taguchi H. J. Biol. Chem. 266:12588-12594(1991) [PubMed: 1840590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026. |
| [2] | "Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase." Stoll V.S., Kimber M.S., Pai E.F. Structure 4:437-447(1996) [PubMed: 8740366] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D90339 Genomic DNA. Translation: BAA14352.1. |
| PIR | A40885. |
3D structure databases | |
| ProteinModelPortal | P26298. |
| SMR | P26298. Positions 1-330. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LDHD_LACPE | ||||||||
| Accession | Primary (citable) accession number: P26298 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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