A0A7X2LQL2 · A0A7X2LQL2_9BURK
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids310 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of lactate to pyruvate.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic activity
- (S)-lactate + NAD+ = pyruvate + NADH + H+
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 | 7-12 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAVG | ||||||
Binding site | 11 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 32 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 76-77 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GV | ||||||
Binding site | 79 | substrate | ||||
Sequence: Q | ||||||
Binding site | 85 | substrate | ||||
Sequence: R | ||||||
Binding site | 92 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 115-117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ATN | ||||||
Binding site | 117-120 | substrate | ||||
Sequence: NPLD | ||||||
Binding site | 140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 145-148 | substrate | ||||
Sequence: DSAR | ||||||
Binding site | 150 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 165 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: H | ||||||
Active site | 172 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 227 | 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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Telluria group > Pseudoduganella
Accessions
- Primary accessionA0A7X2LQL2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 218 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-139 | Lactate/malate dehydrogenase N-terminal | ||||
Sequence: MKIGIVGAGAVGGAAAFALINQGIGSEIVLVDRNAALAEAQHLDLLHATPYCHPLQVRCGGFEDLAGCALVILAAGVSQAPGETRLQLLERNAAVFRAIVPAVVRHAPDAVLLVATNPLDVMTHVALRISGLPPARVIG | ||||||
Domain | 142-304 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TLLDSARFRALLAGRLGVATASVHAQVLGEHGDSEVLVWSGAQVAGMPLQRFAALQGVRLDGATMADIDTGVRRAAYRIIDGKGATCYGIGAALAMLARCVLFDEKRVLTVSTHWGDIDGVPDVTLSMPVQVGAQGATFHIPPALSDTEQQALADSARVIRAT |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length310
- Mass (Da)32,075
- Last updated2021-06-02 v1
- Checksum71F93AFC93758456