Q99JY0 · ECHB_MOUSE
- ProteinTrifunctional enzyme subunit beta, mitochondrial
- GeneHadhb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids475 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoAThis reaction proceeds in the backward direction.
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 139 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Site | 429 | Increases nucleophilicity of active site Cys | ||||
Sequence: H | ||||||
Active site | 459 | Proton donor/acceptor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | mitochondrial fatty acid beta-oxidation multienzyme complex | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Molecular Function | acetyl-CoA C-acyltransferase activity | |
Molecular Function | acetyl-CoA C-myristoyltransferase activity | |
Molecular Function | lncRNA binding | |
Molecular Function | protein-containing complex binding | |
Biological Process | cellular response to lipopolysaccharide | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | gene expression |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrifunctional enzyme subunit beta, mitochondrial
- Alternative names
Including 1 domain:
- Recommended name3-ketoacyl-CoA thiolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99JY0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Protein stability and association with membranes require HADHA.
Features
Showing features for intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Intramembrane | 174-221 | |||||
Sequence: IRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-34 | Mitochondrion | ||||
Sequence: MTTILTSTFRNLSTTSKWALRSSIRPLSCSSQLH | ||||||
Chain | PRO_0000034082 | 35-475 | Trifunctional enzyme subunit beta, mitochondrial | |||
Sequence: SAPAVQTKSKKTLAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK | ||||||
Modified residue | 53 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 73 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 73 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 189 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 189 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 191 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 273 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 292 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 294 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 294 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 299 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 333 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 333 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 349 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 362 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.
Keywords
- PTM
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).
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
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)51,386
- Last updated2001-06-01 v1
- ChecksumF131B497C4F5FAF4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YXU1 | D3YXU1_MOUSE | Hadhb | 173 | ||
A0A0G2JER1 | A0A0G2JER1_MOUSE | Hadhb | 41 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 24-25 | in Ref. 1; BAC36493 | ||||
Sequence: IR → HK | ||||||
Sequence conflict | 425 | in Ref. 1; BAC38790 | ||||
Sequence: L → M | ||||||
Sequence conflict | 450 | in Ref. 1; BAC38790 | ||||
Sequence: G → R | ||||||
Sequence conflict | 450 | in Ref. 1; BAC39015 | ||||
Sequence: G → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |