A0A1C5Q3J8 · A0A1C5Q3J8_9CLOT
- ProteinL-lactate dehydrogenase
- Geneldh_1
- 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 | 25-30 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 29 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 50 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 55 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 80 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 94-95 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 97 | substrate | |||
Binding site | 103 | substrate | |||
Binding site | 110 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 116 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 133-135 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 135-138 | substrate | |||
Binding site | 158 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 163-166 | substrate | |||
Binding site | 168 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Binding site | 183 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Active site | 190 | Proton acceptor | |||
Binding site | 245 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
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
- Strains
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium > environmental samples
Accessions
- Primary accessionA0A1C5Q3J8
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 21-43 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 236 | Phosphotyrosine | |||
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 20-157 | Lactate/malate dehydrogenase N-terminal | |||
Domain | 160-326 | Lactate/malate dehydrogenase C-terminal | |||
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length328
- Mass (Da)35,402
- Last updated2016-11-02 v1
- MD5 Checksum99046313C4DF4A281EEA576FC5238B23
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FMER01000005 EMBL· GenBank· DDBJ | SCH43736.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FMGK01000006 EMBL· GenBank· DDBJ | SCI90480.1 EMBL· GenBank· DDBJ | Genomic DNA |