A0A1C0U653 · A0A1C0U653_9GAMM

Function

function

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.

Caution

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

Catalytic activity

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Features

Showing features for site, binding site, active site.

Type
IDPosition(s)Description
Site119Important for catalytic activity
Site139Important for catalytic activity
Binding site296substrate
Binding site324NAD+ (UniProtKB | ChEBI)
Binding site343NAD+ (UniProtKB | ChEBI)
Binding site400-402NAD+ (UniProtKB | ChEBI)
Binding site407NAD+ (UniProtKB | ChEBI)
Binding site429NAD+ (UniProtKB | ChEBI)
Active site450For 3-hydroxyacyl-CoA dehydrogenase activity
Binding site453NAD+ (UniProtKB | ChEBI)
Binding site500substrate
Binding site660substrate

GO annotations

AspectTerm
Cellular Componentfatty acid beta-oxidation multienzyme complex
Molecular Function3-hydroxybutyryl-CoA epimerase activity
Molecular Functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
Molecular Functionenoyl-CoA hydratase activity
Molecular Functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
Molecular FunctionNAD+ binding
Biological Processfatty acid beta-oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid oxidation complex subunit alpha

Including 2 domains:

  • Recommended name
    Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
  • EC number
  • Recommended name
    3-hydroxyacyl-CoA dehydrogenase
  • EC number

Gene names

    • Name
      fadB
    • ORF names
      Ppb6_01307

Organism names

Accessions

  • Primary accession
    A0A1C0U653

Proteomes

Interaction

Subunit

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-189Enoyl-CoA hydratase/isomerase
Region311-7283-hydroxyacyl-CoA dehydrogenase
Domain316-4943-hydroxyacyl-CoA dehydrogenase NAD binding
Domain496-5923-hydroxyacyl-CoA dehydrogenase C-terminal
Domain627-6913-hydroxyacyl-CoA dehydrogenase C-terminal

Sequence similarities

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    728
  • Mass (Da)
    79,321
  • Last updated
    2016-11-02 v1
  • MD5 Checksum
    E47D698EA0A136B04A4E6EB451899A48
MLYQSETIQVNWLKDGIAELVFNAPAAINKLDTKTVASLDKAVASLEQQTELKGVLLRSEKTAFIVGADITEFLSLFDSPVEKLQEWLDFSNSIFNRIEDLPVPTISAINGYTLGGGCECVLSTDFRVASPDVRIGLPETKLGIMPGFGGSVRLPRLIGTDNALDIIAAGKDIGAEEALKNGLIDAVISNEKLIDSAVSMLEQAIAGDLDWKAARQPKLEPLKLNEIERGMSFSVAKGMVMKVAGPHYPAPITAVKSIEKAATLGRDEALKQETASFIPLAQTNVARALVGIFLNDQYIKGLAKKHLKEVITPEYAAVLGAGIMGGGIAYQSARKGVPVMMKDISQQALELGMSEAAKLLNKQFERGRLSPIKMALTLSSIQPTLNYAGIEQAQIVVEAVVENPKIKAAVLSETENLVNEDCILASNTSTIPISELANSLKRPENFCGMHFFNPVHRMPLVEIIRGEKTSEKTISTVVAYASKIGKTPIVVNDCPGFFVNRVLLPYLLGFGLLLRDGGDFRQIDKIMEKEFGWPMGPAYLIDVIGLDTAHHAQSVMAQGFPDRMQRDYKDAIDVLYDNQRYGQKNGIGFYKYTQDKKGKPKKEQDEQTDQLLATICQPKNNFSGEEIIARTMIPMINEVVRCLEEGVIASPAEADMALVYGLGFPPFRGGVFRYLETMGTAAYVKMAENYAHLGALYQVPPGLKAKAERNESYYPIAATIAVSTGTTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LOMY01000039
EMBL· GenBank· DDBJ
OCQ53420.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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