Q8NRY8 · DLD_CORGL

Function

function

Catalyzes the oxidation of D-lactate to pyruvate. Has also weak activity with L-lactate and DL-2-hydroxybutyrate. Electrons derived from D-lactate oxidation enter the electron transport chain. Essential for growth with D-lactate as sole carbon and energy source.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.62 mMD-lactate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
73.5 μmol/min/mg

pH Dependence

Optimum pH is 7.0.

Temperature Dependence

Optimum temperature is 45 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site78-82FAD (UniProtKB | ChEBI)
Binding site86-87FAD (UniProtKB | ChEBI)
Binding site145FAD (UniProtKB | ChEBI)
Binding site152FAD (UniProtKB | ChEBI)
Binding site162FAD (UniProtKB | ChEBI)
Binding site263FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextrinsic component of cytoplasmic side of plasma membrane
Molecular FunctionD-lactate dehydrogenase (quinone) activity
Molecular FunctionFAD binding
Molecular Functionquinone binding
Biological Processlactate oxidation
Biological Processrespiratory electron transport chain
Biological Processtransmembrane transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Quinone-dependent D-lactate dehydrogenase
  • EC number
  • Alternative names
    • D-lactate dehydrogenase
      (D-LDH
      )

Gene names

    • Name
      dld
    • Ordered locus names
      Cgl0901

Organism names

Accessions

  • Primary accession
    Q8NRY8
  • Secondary accessions
    • Q6M6P4

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Inactivation results in the loss of the ability to grow with D-lactate.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004417061-571Quinone-dependent D-lactate dehydrogenase

Keywords

Expression

Induction

Constitutively expressed.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain44-273FAD-binding PCMH-type

Sequence similarities

Belongs to the quinone-dependent D-lactate dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    571
  • Mass (Da)
    63,723
  • Last updated
    2002-10-01 v1
  • Checksum
    55DE9D87A864264F
MTQPGQTTTTSHEAIDAFKRIVGDEHVLTSERATMPFSKGYRFGGGPVFAVVRPGTLVEMWRALQVSVDNNLIVIPQASNTGLTGGSGPGFQDYDRPIVIISTHRIDEVHLINDAREAISLAGTPLTHLTDALAKHQREPHSVIGSTSIGASVIGGIANNSGGSQIRKGPAFTREAIFARVNDDGKVELVNHLGISLGDDPEVALDRLQRGEWSPEDVTPAPEDSNETEYAEHLRKIVPSPARYNANPEYLFEASGSAGKLMVFAVRTRTFPREVHPTVFYIGTNNTHELEEIRRLFLEADMPLPISGEYMGRSAFDLAEKYGKDTFVFLKFMSPALQTRMFSFKTWANGLFSKIPGIGPTFADTVSQAMFSVLPNQLPKRMMEYRNRFEHHLLLTVSESQKAASEKMLKEFFAEPEHTGEFFICTSDEEKSASLNRFGAASAATRYAALKRRHIAGLIPIDVALRRDDWNWLEVLPEEIDDQLEVKAYYGHFFCHVMHQDYVAKQGVDLEALHDRIQHLLEERGAKLPAEHNYGRIYKLPESMEEHFKELDPTNTFNAGIGGTSPHKDWA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000036
EMBL· GenBank· DDBJ
BAB98294.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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