A0A1E5LFQ0 · A0A1E5LFQ0_9BACI
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids315 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of lactate to pyruvate.
Catalytic activity
- (S)-lactate + NAD+ = H+ + NADH + pyruvate
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) | ||||
Sequence: GTGFVG | ||||||
Binding site | 16 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 37 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 68 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 82-83 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 85 | substrate | ||||
Sequence: Q | ||||||
Binding site | 91 | substrate | ||||
Sequence: R | ||||||
Binding site | 98 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 104 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 121-123 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ATN | ||||||
Binding site | 123-126 | substrate | ||||
Sequence: NPVD | ||||||
Binding site | 146 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 151-154 | substrate | ||||
Sequence: DTAR | ||||||
Binding site | 156 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 171 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: H | ||||||
Active site | 178 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 232 | substrate | ||||
Sequence: T |
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
Accessions
- Primary accessionA0A1E5LFQ0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 223 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-145 | Lactate/malate dehydrogenase N-terminal | ||||
Sequence: RVALIGTGFVGSSYAFALLNQGIVEELVLIDANEEKACGDAMDLNHGLAFAPSSMKIWSGTYEDCKDADLVVITAGANQKPGETRLDLVEKNAAIFKTIVTSVMESGFDGIFLVATNPVDIMTYATWKYSGLPKERVIG | ||||||
Domain | 148-313 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TILDTARLRFLTGQYFEIDTRNVHAYVIGEHGDTELPVWSLAKVGGRSVCELVEENEQYKNEDLDDIFVNVRDAAYHIINRKGATYYGIAMGMVRLTKAVLNNENSILTVSAYLEGEYGQNDVYVGVPAVVNRNGLREVIEINLNEKEKEQFKHSAEVLKKTMAPI |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)34,733
- Last updated2017-01-18 v1
- ChecksumCFDCE04F0DCE3836
Keywords
- Technical term