Q99JY0 · ECHB_MOUSE

  • Protein
    Trifunctional enzyme subunit beta, mitochondrial
  • Gene
    Hadhb
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.

Catalytic activity

  • acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
    This reaction proceeds in the backward direction.
    EC:2.3.1.16 (UniProtKB | ENZYME | Rhea)
  • acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
    EC:2.3.1.155 (UniProtKB | ENZYME | Rhea)

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site139Acyl-thioester intermediate
Site429Increases nucleophilicity of active site Cys
Active site459Proton donor/acceptor

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentmitochondrial fatty acid beta-oxidation multienzyme complex
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial nucleoid
Cellular Componentmitochondrial outer membrane
Cellular Componentmitochondrion
Molecular Functionacetyl-CoA C-acetyltransferase activity
Molecular Functionacetyl-CoA C-acyltransferase activity
Molecular Functionacetyl-CoA C-myristoyltransferase activity
Molecular FunctionlncRNA binding
Molecular Functionprotein-containing complex binding
Biological Processcellular response to lipopolysaccharide
Biological Processfatty acid beta-oxidation
Biological Processgene expression

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Trifunctional enzyme subunit beta, mitochondrial
  • Alternative names
    • TP-beta

Including 1 domain:

  • Recommended name
    3-ketoacyl-CoA thiolase
  • EC number
  • Alternative names
    • Acetyl-CoA acyltransferase
    • Beta-ketothiolase

Gene names

    • Name
      Hadhb

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q99JY0
  • Secondary accessions
    • Q3TEH9
    • Q8BJI5
    • Q8BJM0
    • Q8BK52

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for intramembrane.

TypeIDPosition(s)Description
Intramembrane174-221

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-34Mitochondrion
ChainPRO_000003408235-475Trifunctional enzyme subunit beta, mitochondrial
Modified residue53N6-succinyllysine
Modified residue73N6-acetyllysine; alternate
Modified residue73N6-succinyllysine; alternate
Modified residue189N6-acetyllysine; alternate
Modified residue189N6-succinyllysine; alternate
Modified residue191N6-succinyllysine
Modified residue273N6-succinyllysine
Modified residue292N6-succinyllysine
Modified residue294N6-acetyllysine; alternate
Modified residue294N6-succinyllysine; alternate
Modified residue299N6-acetyllysine
Modified residue333N6-acetyllysine; alternate
Modified residue333N6-succinyllysine; alternate
Modified residue349N6-acetyllysine
Modified residue362N6-acetyllysine

Post-translational modification

Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits; forms the mitochondrial trifunctional enzyme (By similarity).
Also purified as higher order heterooligomers including a 4 alpha/HADHA and 4 beta/HADHB heterooligomer which physiological significance remains unclear (By similarity).
The mitochondrial trifunctional enzyme interacts with MTLN (PubMed:29949755).
Interacts with RSAD2/viperin (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    475
  • Mass (Da)
    51,386
  • Last updated
    2001-06-01 v1
  • Checksum
    F131B497C4F5FAF4
MTTILTSTFRNLSTTSKWALRSSIRPLSCSSQLHSAPAVQTKSKKTLAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YXU1D3YXU1_MOUSEHadhb173
A0A0G2JER1A0A0G2JER1_MOUSEHadhb41

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict24-25in Ref. 1; BAC36493
Sequence conflict425in Ref. 1; BAC38790
Sequence conflict450in Ref. 1; BAC38790
Sequence conflict450in Ref. 1; BAC39015

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK033462
EMBL· GenBank· DDBJ
BAC28300.1
EMBL· GenBank· DDBJ
mRNA
AK076814
EMBL· GenBank· DDBJ
BAC36493.1
EMBL· GenBank· DDBJ
mRNA
AK083164
EMBL· GenBank· DDBJ
BAC38790.1
EMBL· GenBank· DDBJ
mRNA
AK083767
EMBL· GenBank· DDBJ
BAC39015.1
EMBL· GenBank· DDBJ
mRNA
AK150889
EMBL· GenBank· DDBJ
BAE29936.1
EMBL· GenBank· DDBJ
mRNA
AK169637
EMBL· GenBank· DDBJ
BAE41269.1
EMBL· GenBank· DDBJ
mRNA
BC005585
EMBL· GenBank· DDBJ
AAH05585.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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