O17953 · DLDH_CAEEL

  • Protein
    Dihydrolipoyl dehydrogenase, mitochondrial
  • Gene
    dld-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Miscellaneous

The active site is a redox-active disulfide bond.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for binding site, active site.

149550100150200250300350400450
Type
IDPosition(s)Description
Binding site59-68FAD (UniProtKB | ChEBI)
Binding site77FAD (UniProtKB | ChEBI)
Binding site169-171FAD (UniProtKB | ChEBI)
Binding site206-213NAD+ (UniProtKB | ChEBI)
Binding site229NAD+ (UniProtKB | ChEBI)
Binding site264NAD+ (UniProtKB | ChEBI)
Binding site299NAD+ (UniProtKB | ChEBI)
Binding site340FAD (UniProtKB | ChEBI)
Binding site346-349FAD (UniProtKB | ChEBI)
Active site472Proton acceptor

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Cellular Componentoxoglutarate dehydrogenase complex
Molecular Functiondihydrolipoyl dehydrogenase activity
Molecular Functionflavin adenine dinucleotide binding
Biological Processfatty acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrolipoyl dehydrogenase, mitochondrial
  • EC number
  • Alternative names
    • Dihydrolipoamide dehydrogenase

Gene names

    • Name
      dld-1
    • ORF names
      LLC1.3

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    O17953
  • Secondary accessions
    • D3YT81

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, transit peptide, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_0000421278?-495Dihydrolipoyl dehydrogenase, mitochondrial
Transit peptide1-?Mitochondrion
Disulfide bond68↔73Redox-active

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

O17953-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    495
  • Mass (Da)
    52,633
  • Last updated
    2003-03-01 v2
  • Checksum
    77EB4A2FA935F0F6
MSLSRTTQLPFAKRQFFQVLARNYSNTQDADLVVIGGGPGGYVAAIKAAQLGMKTVCVEKNATLGGTCLNVGCIPSKALLNNSHYLHMAQHDFAARGIDCTASLNLPKMMEAKSNSVKQLTGGIKQLFKANKVGHVEGFATIVGPNTVQAKKNDGSVETINARNILIASGSEVTPFPGITIDEKQIVSSTGALSLGQVPKKMVVIGAGVIGLELGSVWQRLGAEVTAVEFLGHVGGMGIDGEVSKNFQRSLTKQGFKFLLNTKVMGASQNGSTITVEVEGAKDGKKQTLECDTLLVSVGRRPYTEGLGLSNVQIDLDNRGRVPVNERFQTKVPSIFAIGDVIEGPMLAHKAEDEGILCVEGIAGGPVHIDYNCVPSVVYTHPEVAWVGKAEEQLKQEGVAYKIGKFPFVANSRAKTNNDQEGFVKVLADKQTDRMLGVHIIGPNAGEMIAEATLAMEYGASAEDVARVCHPHPTLSEAFREANLAAYCGKAINNV

O17953-2

  • Name
    b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0453811-345in isoform b

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z82277
EMBL· GenBank· DDBJ
CAB05249.2
EMBL· GenBank· DDBJ
Genomic DNA
Z82277
EMBL· GenBank· DDBJ
CBK19462.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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