A0A5J6Z8B2 · A0A5J6Z8B2_9CORY
- ProteinL-lactate dehydrogenase
- GeneldhA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (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 | 13-18 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGDVG | ||||||
Binding site | 17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
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: GV | ||||||
Binding site | 86 | substrate | ||||
Sequence: Q | ||||||
Binding site | 92 | substrate | ||||
Sequence: R | ||||||
Binding site | 99 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
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 | 172 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: H | ||||||
Active site | 179 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 240 | 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 > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionA0A5J6Z8B2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 231 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-146 | Lactate/malate dehydrogenase N-terminal | ||||
Sequence: KIVLIGAGDVGIAYAYALVNQGLCDHLAIIDINERKTWGHVQDLNHAVPWAGHSVKVSVGTYEDCADAAVVVNCAGVAQKPGETRLDLVGRNVAIFEDIVGKVMASGFNGIFLVATNPVDILSFATWKLSGLPSSQVIG | ||||||
Domain | 149-318 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TILDTARYRYSLGRYFDLAPSSVHAYVIGEHGDTELPVLSAGSAGGVPLKKMLRARAEEKAQDGALPIDDASAIFEETRDAAYEIIQAKGSTSFGIGMGLARITRAILHNQDVVLPVSAFLEGHYGLEDVYIGTPAVIDRRGVRHVVELDLDEDENQKFQHSARVLKDVM |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)35,555
- Last updated2019-12-11 v1
- ChecksumDC99B1B2B1A53375
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP045032 EMBL· GenBank· DDBJ | QFQ01579.1 EMBL· GenBank· DDBJ | Genomic DNA |