A0A852MRR9 · A0A852MRR9_9PASS

  • Protein
    Peroxisomal acyl-coenzyme A oxidase 1
  • Gene
    Acox1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

Caution

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

Catalytic activity

  • (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + O2 = (2E,5Z,8Z,11Z,14Z,17Z)-icosahexaenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + O2 = (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • octadecanoyl-CoA + O2 = (2E)-octadecenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • octanoyl-CoA + O2 = (2E)-octenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • tetracosanoyl-CoA + O2 = (2E)-tetracosenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • tetradecanoyl-CoA + O2 = (2E)-tetradecenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
    EC:1.3.3.6 (UniProtKB | ENZYME | Rhea)
  • decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.
  • hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site144FAD (UniProtKB | ChEBI)
Binding site183FAD (UniProtKB | ChEBI)
Active site426Proton acceptor

GO annotations

AspectTerm
Cellular Componentperoxisome
Molecular FunctionFAD binding
Molecular Functionfatty acid binding
Molecular Functionpalmitoyl-CoA oxidase activity
Biological Processfatty acid beta-oxidation using acyl-CoA oxidase
Biological Processlipid homeostasis
Biological Processvery long-chain fatty acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxisomal acyl-coenzyme A oxidase 1
  • EC number
  • Alternative names
    • Palmitoyl-CoA oxidase
    • Peroxisomal fatty acyl-CoA oxidase
    • Straight-chain acyl-CoA oxidase

Gene names

    • Name
      Acox1
    • ORF names
      PTEMEL_R13770

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B10K-IZ-033-77
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Sylvioidea > Timaliidae > Pteruthius

Accessions

  • Primary accession
    A0A852MRR9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-138Acyl-coenzyme A oxidase N-terminal
Domain141-249Acyl-CoA oxidase/dehydrogenase middle
Domain280-441Acyl-CoA oxidase C-alpha1
Domain484-662Acyl-CoA oxidase C-terminal

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    666
  • Mass (Da)
    74,787
  • Last updated
    2021-09-29 v1
  • Checksum
    CBE99FE23D18E2E2
AAAMAVNADLRRERAAATFQPELLTHILDGGPERTRRRKEIEALVLNDPDFQHEDLNFLSRSQRYEQAIRKSSLMVMKLREYGIADPEEIYWFKSFVHRGRPEPLDLHLGMFLPTLLTQATPEQQDRFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPSTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLYTQGQCKGLHAFIVPIRQLGTHEPLPGITVGDIGPKFGYDEMDNGYLKMDNFRIPRENMLMKYAQVEPDGTYVKPVSDKLTYGTMVFIRSLIVGDSARSLSRACTIAIRYSAVRHQSELKPGEPEPQILDYQTQQYKLFPLLATAYAFHFVGAYIKDTYHRISGDISKGDLSELPELHALTAGLKAFTSWTANAGIEECRMACGGHGYSRCSGIPDIYVTFTPSCTYEGENTVMMLQTARFLMKSYTQVTSGQQVTGMVSYLNDLSRQRIQPQHVAARTVTVRINDPTSLVEAYKSRAARLVESAAKNLQAELNHRKSKEDAWNRTSVDLVRASEAHCHYVIVKLFSAKLAEVSDAAVCAVLTDLCLLYALFGISRNTGDFLQAGILTSAQITQVNQHVKELLAVIRPNAVALVDSFDFHDVHLGSVLGRYDGNVYENMFEWAKKSPLNKTQVHESFHKHLKPMQAKL

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue666

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEIY01000375
EMBL· GenBank· DDBJ
NXY07260.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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