A0AAJ1XTY9 · A0AAJ1XTY9_9ENTE
- ProteinL-lactate dehydrogenase
- Geneldh
- 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+ = 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 | 21 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 42 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 47 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 72 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 86-87 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 89 | substrate | ||||
Sequence: Q | ||||||
Binding site | 95 | substrate | ||||
Sequence: R | ||||||
Binding site | 125-127 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AAN | ||||||
Binding site | 127-130 | substrate | ||||
Sequence: NPVD | ||||||
Binding site | 150 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 155-158 | substrate | ||||
Sequence: DSAR | ||||||
Binding site | 160 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 175 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: H | ||||||
Active site | 182 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 236 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | oxidoreductase activity |
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 > Lactobacillales > Enterococcaceae > Enterococcus
Accessions
- Primary accessionA0AAJ1XTY9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 227 | Phosphotyrosine | ||||
Sequence: Y |
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 | ||||
Sequence: KVILVGDGAVGSSYAFALVTQNIAQEVGIIDINVPKTEGDALDLSHALAFTSPKKIYAATYDDCHDADLVVLTAGAPQKPGETRLDLVHKNLKINKEIVTTIVDSGFNGIFLVAANPVDILTYSTWKFSGFPKERVIG | ||||||
Domain | 152-320 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TSLDSARFRQAIAELVDVDARNVHAYILGEHGDTEFPVWSHANVAGLQIYEWVKNNPDVDEEAMVNLFFNVRDAAYTIIEKKGATFYGIAVALARITKAILNDENSVLPLSVYLEGEYGQNDIYIGAPAIINRQGVKQVIEIPLTDAEQEKMEASASALKEVIETAFAK |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)35,487
- Last updated2024-07-24 v1
- ChecksumE7D6F6D13D0C07AB