P00344 · LDH_GEOSE
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids317 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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). The improvement in affinity for substrate occurs in two steps; the binding of fructose 1,6-bisphosphate (FBP) to the dimer, and the dimer to tetramer conversion.
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 | 16-17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FV | ||||||
Binding site | 38 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 43 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 69 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 83-84 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 86 | substrate | ||||
Sequence: Q | ||||||
Binding site | 92 | substrate | ||||
Sequence: R | ||||||
Binding site | 105 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 122-124 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ATN | ||||||
Binding site | 124-127 | substrate | ||||
Sequence: NPVD | ||||||
Binding site | 147 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 152-155 | substrate | ||||
Sequence: DTAR | ||||||
Binding site | 157 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 169-172 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: QNVH | ||||||
Active site | 179 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 233 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-lactate dehydrogenase activity | |
Molecular Function | NAD binding | |
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 > Geobacillus
Accessions
- Primary accessionP00344
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 157 | This mutant undergoes a reversible subunit assembly from dimer to tetramer. However, the tetramer mutant is much more stable than the wild type, and is destabilized rather than stabilized by binding the allosteric regulator, fructose 1,6-bisphosphate (FBP). The mutation weakens the binding of fructose 1,6-bisphosphate (FBP) to both the dimeric and tetrameric forms, and almost abolishes any stimulatory effect. | ||||
Sequence: R → Q |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000168328 | 1-317 | L-lactate dehydrogenase | |||
Sequence: MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKLVESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFTR | ||||||
Modified residue | 224 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Exists as a dimer and a tetramer (dimer of dimers). The conversion occurs via the binding of fructose 1,6-bisphosphate (FBP) to the dimer.
Structure
Sequence
- Sequence statusComplete
- Length317
- Mass (Da)34,863
- Last updated1988-01-01 v1
- Checksum4B146CF681C91046
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 113 | in Ref. 2; AAA22567 | ||||
Sequence: S → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M14788 EMBL· GenBank· DDBJ | AAA22568.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M19396 EMBL· GenBank· DDBJ | AAA22567.1 EMBL· GenBank· DDBJ | Genomic DNA |