A0A640MU78 · A0A640MU78_BACAN
- ProteinL-lactate dehydrogenase
- Geneldh1_1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids327 (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 | 17-22 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 21 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 47 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 72 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 86-87 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 89 | substrate | |||
Binding site | 95 | substrate | |||
Binding site | 102 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 125-127 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 127-130 | substrate | |||
Binding site | 150 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 155-158 | substrate | |||
Binding site | 160 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Binding site | 175 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | |||
Active site | 182 | Proton acceptor | |||
Binding site | 236 | 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 > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionA0A640MU78
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 227 | Phosphotyrosine | |||
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 12-149 | Lactate/malate dehydrogenase N-terminal | |||
Domain | 152-320 | Lactate/malate dehydrogenase C-terminal | |||
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)35,487
- Last updated2020-04-22 v1
- MD5 ChecksumF02B3353B3673D64690379650484F2D0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BLEY01000041 EMBL· GenBank· DDBJ | GEU17534.1 EMBL· GenBank· DDBJ | Genomic DNA |