A0A292IHL4 · A0A292IHL4_9MOLU
- ProteinL-lactate dehydrogenase
- Geneldh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids313 (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
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 | 11-16 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSGNVG | ||||||
Binding site | 15 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 36 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 67 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 81-82 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GL | ||||||
Binding site | 84 | substrate | ||||
Sequence: Q | ||||||
Binding site | 90 | substrate | ||||
Sequence: R | ||||||
Binding site | 97 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 120-122 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ASN | ||||||
Binding site | 122-125 | substrate | ||||
Sequence: NPLD | ||||||
Binding site | 145 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 150-153 | substrate | ||||
Sequence: DTAR | ||||||
Active site | 177 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 231 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-lactate dehydrogenase activity | |
Biological Process | glycolytic 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 > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionA0A292IHL4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 222 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-144 | Lactate/malate dehydrogenase N-terminal | ||||
Sequence: VKVVLIGSGNVGSSFLYAAINQGLSRSYGIIDINSTLRDAQVLDFEDSAWNNPVDFKIHAANYADLKNTEYLVITAGLPQKPGQTRLELAGANVKIMKEIARQVKESGFSGYTIIASNPLDVMTYTYLKTTGFPKNKVIG | ||||||
Domain | 147-310 | Lactate/malate dehydrogenase C-terminal | ||||
Sequence: TTLDTARLRSFISRRMNVSNNSVQAFILGEHGDSSVTLFSQIKIDGIPFKNFENIHGINENNYETLLETPVRQKAYEIIKGKGSTYYGIGSALAYILKALINGTDEILPVCAYLDGEYGIHDVCVGVPSIVGKDGIAKVIEYPMNDKELKKFHASVDIIKKYNQ |
Sequence similarities
Belongs to the LDH/MDH superfamily. LDH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length313
- Mass (Da)34,416
- Last updated2017-12-20 v1
- Checksum15828BADA42B0A13
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG937516 EMBL· GenBank· DDBJ | CDN40173.1 EMBL· GenBank· DDBJ | Genomic DNA |