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.

A0A6G0UDY8 · A0A6G0UDY8_9BILA

Function

function

Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • hexacosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-hexacosenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • tetracosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • tricosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-tricosenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • a 2,3-saturated acyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • docosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • eicosanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Lipid metabolism; fatty acid beta-oxidation.

GO annotations

AspectTerm
Cellular Componentmitochondrial membrane
Molecular Functionacyl-CoA dehydrogenase activity
Molecular Functionflavin adenine dinucleotide binding
Biological Processfatty acid beta-oxidation using acyl-CoA dehydrogenase

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Acyl-CoA dehydrogenase family member 11

Gene names

    • ORF names
      FO519_009504

Organism names

  • Taxonomic identifier
  • Strain
    • NKZ332
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Halicephalobus

Accessions

  • Primary accession
    A0A6G0UDY8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain227-453Aminoglycoside phosphotransferase
Domain574-697Acyl-CoA dehydrogenase/oxidase N-terminal
Domain701-804Acyl-CoA oxidase/dehydrogenase middle
Domain830-919Acyl-CoA dehydrogenase/oxidase C-terminal

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    920
  • Mass (Da)
    104,128
  • Last updated
    2020-08-12 v1
  • MD5 Checksum
    A481B5AFFE55717C164D838CAB72FF47
KERELGLEPGSIAKTVVSKEVFPEFEALERGETNLEDFHAVFTHFYNKQNNRNDRTIIDFFRDFYESGIGIDKRWTKVLQALKSEGIKVAVLTNNGFRDRGKKKKTHLLDEKLFDGIFESCRIGSRKPEKQIFEHVLKAIKTKPEETLFIDDLGGNLKGAAAVGIDTLRFKLDEDDFQIISEKVGIDFENIIPGTRNPGEKEKLSEDVLRKYLSEKFGINVNEKLVIKKFGHGQSNPTYYVKFGSREFALRKKPSGKLLPSAHLIDREYRLIKALENEIPLPKALDYVEGVLDTPFYLMDYCRGRIFLNPEVPEVGKENRRKIYEKMIQVLAEIHNVDYKKSGLGDYGKEGGYMARNLERWKKQYESSKTEDIPIISELFSWLESNVPVQRKTTIIHGDFRLDNLIFFDKKDEVEAVLDWELSTLGDPFSDLSTALLGHYNPLSGTPLPALGKKNLSNLGIPDVKDLLEIYYKSTNQEPLKDSEWAFYMAFVCFRYAAIAQGVYKRFLQGQASSTQAGKFGAMPKLLAELGMKIIKDAEKNQNTGKVGNERNSGKTVFGFFPIFPEALSGKAAKIHKEVKEFINEKVIPNEIKIEEYFSDPEKKWTVNPMIEDLKDEAKRNGLWNIFISNTIDPENRYGIGLTNVEYSHICEEMGKSIFAPEIFNSNAPDSGNMEVLMKFGTETQKKEFLDPLLEGKIRSCFSMTEPDVASSDAVNIQGSIVRDGENLVINSKKWFITGAGHPNCKFTIFMGRMSGWKKMPAHKQQSMVLIPMDTPGVKVVRPLSVFGIQDPPYGHCEVLFENVVVPYSNLILGEGRGFEIAQGRLGPGRIHHSRLLVLKAAHLMDTVGIKKAISEISMIKVLCPQMALRVVDRSIQIHGAAGLSQDFPMSNFFTWARALRQADGPDIVHIETVAKNLLK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VOSG01001045
EMBL· GenBank· DDBJ
KAE9547284.1
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