Ldhd
entrez
52815
canonical
uniprot
Q7TNG8
canonical
ensembl
ENSMUSG00000031958
resolver
ensp
ENSMUSP00000068086
resolver
enst
ENSMUST00000070004
resolver
genesymbol
Ldhd
resolver
genesymbol_syn
mLDHD
resolver
uniprot
Q8BYU7
resolver
uniprot
Q8CIV4
resolver
uniprot_entry
LDHD_MOUSE
resolver
uniprot_sec
Q8BYU7
resolver
uniprot_sec
Q8CIV4
resolver
amino_acid_sequence
MAMLLRVATQRLSPWRSFCSRGSQGGLSQDFVEALKAVVGSPHVSTASAVREQHGHDESMHRCQPPDAVVWPQNVDQVSRVASLCYNQGVPIIPFGTGTGVEGGVCAVQGGVCINLTHMDQITELNTEDFSVVVEPGVTRKALNTHLRDSGLWFPVDPGADASLCGMAATGASGTNAVRYGTMRDNVINLEVVLPDGRLLHTAGRGRHYRKSAAGYNLTGLFVGSEGTLGIITSTTLRLHPAPEATVAATCAFPSVQAAVDSTVQILQAAVPVARIEFLDDVMMDACNRHSKLNCPVAPTLFLEFHGSQQTLAEQLQRTEAITQDNGGSHFSWAKEAEKRNELWAARHNAWYAALALSPGSKAYSTDVCVPISRLPEILVETKEEIKASKLTGAIVGHVGDGNFHCILLVDPDDAEEQRRVKAFAENLGRRALALGGTCTGEHGIGLGKRQLLQEEVGPVGVETMRQLKNTLDPRGLMNPGKVL
uniprot
proteins
ec_number
1.1.98.-
uniprot
proteins
function
FUNCTION: The mitochondrial D-lactate dehydrogenase is a stereoselective dehydrogenase that targets a wide variety of D-2-hydroxyacids, particularly those with small to moderately sized hydrophobic groups attached to the C2 atom. It includes D-lactate which is generated in small amounts either endogenously through the methylglyoxal metabolism pathway or exogenously via intestinal bacterial activity and dietary intake. The dehydrogenase acts specifically on D-lactate, not on its stereoisomer L-lactate, and prevents the toxic accumulation of D-lactate in the organism. By converting branched-chain D-2-hydroxyacids into branched-chain ketoacids, it may indirectly regulate branched-chain amino acid metabolism. {ECO:0000269|PubMed:37863926}.
uniprot
proteins
mass_dalton
51848
uniprot
proteins
mutagenesis
MUTAGEN 228; /note="T->M: Loss of D-lactate dehydrogenase activity. Loss of FAD binding."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 347; /note="R->A: Loss of D-lactate dehydrogenase activity."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 347; /note="R->W: Loss of D-lactate dehydrogenase activity. No effect on FAD binding."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 351; /note="W->C: Loss of D-lactate dehydrogenase activity. No effect on FAD binding."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 398; /note="H->A: Loss of D-lactate dehydrogenase activity."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 405; /note="H->A: Loss of D-lactate dehydrogenase activity. Loss of Mn(2+) binding."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 440; /note="T->M: Loss of D-lactate dehydrogenase activity. Loss of FAD binding."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 442; /note="E->A: Loss of D-lactate dehydrogenase activity."; /evidence="ECO:0000269|PubMed:37863926"; MUTAGEN 443; /note="H->A: Loss of D-lactate dehydrogenase activity."; /evidence="ECO:0000269|PubMed:37863926
uniprot
proteins
protein_family
FAD-binding oxidoreductase/transferase type 4 family
uniprot
proteins
pubmed
12127981
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
37863926
uniprot
proteins
sequence_length
484
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12127981}.
uniprot
proteins