W4RNN3 · W4RNN3_9BACI
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids316 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of lactate to pyruvate.
Catalytic activity
- (S)-lactate + NAD+ = pyruvate + NADH + H+
Activity regulation
Allosterically activated by fructose 1,6-bisphosphate (FBP).
Pathway
Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 12-17 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 16 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 37 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 68 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 82-83 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 85 | substrate | |||
Binding site | 91 | substrate | |||
Binding site | 98 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 104 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 121-123 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 123-126 | substrate | |||
Binding site | 146 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 151-154 | substrate | |||
Binding site | 156 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Binding site | 171 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Active site | 178 | Proton acceptor | |||
Binding site | 232 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-lactate dehydrogenase activity | |
Biological Process | glycolytic process | |
Biological Process | lactate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-lactate dehydrogenase
- EC number
- Short namesL-LDH
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Mesobacillus
Accessions
- Primary accessionW4RNN3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-23 | ||||
Chain | PRO_5039197544 | 24-316 | L-lactate dehydrogenase | ||
Modified residue | 223 | Phosphotyrosine | |||
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-145 | Lactate/malate dehydrogenase N-terminal | |||
Domain | 148-314 | Lactate/malate dehydrogenase C-terminal | |||
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length316
- Mass (Da)35,093
- Last updated2014-03-19 v1
- Checksum333A49C4EF5F332F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BAUW01000034 EMBL· GenBank· DDBJ | GAE46035.1 EMBL· GenBank· DDBJ | Genomic DNA |