Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A517D374 · A0A517D374_LIMRT

Function

Features

Showing features for binding site, active site.

131020406080100120140160180200220240260280300
Type
IDPosition(s)Description
Binding site9-14NAD+ (UniProtKB | ChEBI)
Binding site34NAD+ (UniProtKB | ChEBI)
Binding site121-123NAD+ (UniProtKB | ChEBI)
Active site178Proton acceptor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionL-lactate dehydrogenase activity
Biological Processlactate metabolic process
Biological Processpyruvate metabolic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • L-lactate dehydrogenase

Gene names

    • ORF names
      FOD75_01040

Organism names

Accessions

  • Primary accession
    A0A517D374

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-145Lactate/malate dehydrogenase N-terminal
Domain148-304Lactate/malate dehydrogenase C-terminal

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    310
  • Mass (Da)
    33,999
  • Last updated
    2019-10-16 v1
  • MD5 Checksum
    40A218AD404D99676C5E2283E4BA94C2
MTRKVGVIGMGNVGSTVAHYIVAMGFSDDLVLIDKNEAKVKADALDFEDAMANLPFHINITVNDYSALKDADVIVSALGNIKLQDNPNADRFAELPFTRQAVKEVAQKIKESGFNGKIVAITNPVDVITSLYQKITGLPKNHVLGTGTLLDSARMKRAVAERLNLDPRSVDGYNLGEHGNSQFTAWSTVRVLGRPLTELADKRGLDLEELDKEAKMGGWTVFQGKKYTNYGVATAAVKLVNAILSDSLTELPVSNFREEYGVYLSYPAVVGRDGVVEQAQLDLTEEELQKLQTSADFIKEKYQESLQAKD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP041676
EMBL· GenBank· DDBJ
QDR71794.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help