A0A510PI38 · A0A510PI38_MICAE
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids331 (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 | 27-32 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GVGQVG | ||||||
Binding site | 31 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 52 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 57 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 97-98 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 100 | substrate | ||||
Sequence: Q | ||||||
Binding site | 106 | substrate | ||||
Sequence: R | ||||||
Binding site | 113 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 136-138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VSN | ||||||
Binding site | 138-141 | substrate | ||||
Sequence: NPVD | ||||||
Binding site | 161 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 166-169 | substrate | ||||
Sequence: DSAR | ||||||
Binding site | 171 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 186 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: H | ||||||
Active site | 193 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 248 | 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 > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis
Accessions
- Primary accessionA0A510PI38
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 239 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-160 | Lactate/malate dehydrogenase N-terminal | ||||
Sequence: VIIGVGQVGMACAYSMLIQDCFDELILQDIATDKVEGEVMDLRHGMPFIEPTDLKMGTVADVGQNADVVIITAGAAQKEGETRLHLLERNVAIFRRILEDVAVYCPSALILVVSNPVDIMTYVTLKITNFPPSRVIG | ||||||
Domain | 163-328 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TVLDSARLRSLLSTQLHVDARNVHAYIIGEHGDSELAVWSSANIGGARLLERDWQDLSAADQESLTEIFLQVKNAAYEIIKRKGYTSYAIGLATTDIVKAILRSQERILTISTLLDGQYGLKDVCLSIPSVVNEKGVIKTLNLALSPRETQQLHNSAKIMRDLIDQ |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length331
- Mass (Da)36,392
- Last updated2019-10-16 v1
- ChecksumFBCEA10A5DE79000