K0ZH94 · K0ZH94_9STRE
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids328 (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 | 14-19 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 18 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 39 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 46 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 71 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 85-86 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 88 | substrate | |||
Binding site | 94 | substrate | |||
Binding site | 101 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 107 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 124-126 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 126-129 | substrate | |||
Binding site | 149 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 154-157 | substrate | |||
Binding site | 159 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Binding site | 174 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Active site | 181 | Proton acceptor | |||
Binding site | 235 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionK0ZH94
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 226 | Phosphotyrosine | |||
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-148 | Lactate/malate dehydrogenase N-terminal | |||
Domain | 151-316 | Lactate/malate dehydrogenase C-terminal | |||
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length328
- Mass (Da)35,283
- Last updated2012-11-28 v1
- MD5 Checksum09A6503751773C6F411A8BC6ACC3AC50
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJRH01000015 EMBL· GenBank· DDBJ | EKA06539.1 EMBL· GenBank· DDBJ | Genomic DNA |