A0A4Q9QQ06 · A0A4Q9QQ06_9PSED
- ProteinL-lactate dehydrogenase
- GenelldD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids379 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.
Catalytic activity
- (S)-lactate + A = AH2 + pyruvate
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 24 | substrate | ||||
Sequence: Y | ||||||
Binding site | 77-79 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PVG | ||||||
Binding site | 106 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 127 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 129 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 129 | substrate | ||||
Sequence: Y | ||||||
Binding site | 155 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 164 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 164 | substrate | ||||
Sequence: R | ||||||
Binding site | 251 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 273 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 275 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 275 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 278 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 278 | substrate | ||||
Sequence: R | ||||||
Binding site | 306-310 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DSGIR | ||||||
Binding site | 306-330 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DSGIRSGLDVVRMIALGADTVMLGR | ||||||
Binding site | 329-330 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | FMN binding | |
Molecular Function | lactate dehydrogenase activity | |
Biological Process | lactate oxidation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-lactate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A4Q9QQ06
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 331-351 | Helical | ||||
Sequence: AFVYALAAAGGAGVSNLLSLI |
Keywords
- Cellular component
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-379 | FMN hydroxy acid dehydrogenase | ||||
Sequence: MIISASTDYRAAAQRRLPPFLFHYIDGGAYAEYTLKRNVEDLASIALRQRVLKNMSELSLETTLFNETLAMPVALAPVGLTGMYARRGEVQAAKAAAEKGIPFTLSTVSVCPIEEVAPAISRPMWFQLYVLKDRGFMKNALERAKAAGVTTLVFTVDMPTPGARYRDAHSGMSGANAAMRRMLQAFTHPAWALDVGLLGKPHDLGNISTYRGHPTGLADYIGWLGANFDPSISWKDLEWIREFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDLKILADSGIRSGLDVVRMIALGADTVMLGRAFVYALAAAGGAGVSNLLSLIEKEMRVAMVLTGAKSIAEISAESLVREL |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)40,777
- Last updated2019-07-31 v1
- ChecksumAB110C16E0B9CDC1