P06149 · DLD_ECOLI
- ProteinQuinone-dependent D-lactate dehydrogenase
- Genedld
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids571 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.
Catalytic activity
- (R)-lactate + a quinone = a quinol + pyruvate
Cofactor
Activity regulation
Inhibited by 2-hydroxy-3-butynoic acid, but not by p-chloromercuribenzoate, n-ethylmaleimide, or 5,5'-dithiobis(2-nitrobenzoic acid).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.16 mM | D-lactate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 76-80 | FAD (UniProtKB | ChEBI) | ||||
Sequence: AANTG | ||||||
Binding site | 84-85 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 143 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 150 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 160 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 262 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | extrinsic component of cytoplasmic side of plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | D-lactate dehydrogenase (quinone) activity | |
Molecular Function | electron transfer activity | |
Molecular Function | FAD binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor | |
Molecular Function | quinone binding | |
Biological Process | aerobic respiration | |
Biological Process | anaerobic respiration | |
Biological Process | lactate oxidation | |
Biological Process | respiratory electron transport chain | |
Biological Process | transmembrane transport |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQuinone-dependent D-lactate dehydrogenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP06149
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Note: May bind the membrane through electrostatic rather than hydrophobic forces.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000079928 | 2-571 | Quinone-dependent D-lactate dehydrogenase | |||
Sequence: SSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 42-213 | FAD-binding PCMH-type | ||||
Sequence: GQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKD | ||||||
Compositional bias | 546-562 | Polar residues | ||||
Sequence: RENDPTNSMNPGIGKTS | ||||||
Region | 546-571 | Disordered | ||||
Sequence: RENDPTNSMNPGIGKTSKRKNWQEVE |
Domain
Contains 3 domains: the flavin adenine dinucleotide (FAD)-binding domain, the cap domain and the membrane-binding domain.
Sequence similarities
Belongs to the quinone-dependent D-lactate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length571
- Mass (Da)64,612
- Last updated2007-01-23 v3
- Checksum77FB2C467CB4389F
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 546-562 | Polar residues | ||||
Sequence: RENDPTNSMNPGIGKTS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M10038 EMBL· GenBank· DDBJ | AAA23688.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X01067 EMBL· GenBank· DDBJ | CAA25531.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00007 EMBL· GenBank· DDBJ | AAA60530.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC75194.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76610.1 EMBL· GenBank· DDBJ | Genomic DNA |