P51660 · DHB4_MOUSE
- ProteinPeroxisomal multifunctional enzyme type 2
- GeneHsd17b4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids735 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bifunctional enzyme acting on the peroxisomal fatty acid beta-oxidation pathway (PubMed:17442273).
Catalyzes two of the four reactions in fatty acid degradation: hydration of 2-enoyl-CoA (trans-2-enoyl-CoA) to produce (3R)-3-hydroxyacyl-CoA, and dehydrogenation of (3R)-3-hydroxyacyl-CoA to produce 3-ketoacyl-CoA (3-oxoacyl-CoA), which is further metabolized by SCPx. Can use straight-chain and branched-chain fatty acids, as well as bile acid intermediates as substrates (By similarity) (PubMed:17442273).
Catalyzes two of the four reactions in fatty acid degradation: hydration of 2-enoyl-CoA (trans-2-enoyl-CoA) to produce (3R)-3-hydroxyacyl-CoA, and dehydrogenation of (3R)-3-hydroxyacyl-CoA to produce 3-ketoacyl-CoA (3-oxoacyl-CoA), which is further metabolized by SCPx. Can use straight-chain and branched-chain fatty acids, as well as bile acid intermediates as substrates (By similarity) (PubMed:17442273).
Miscellaneous
The protein is found both as a full-length peptide and in a cleaved version.
Catalytic activity
- a (3R)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
- (2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoAThis reaction proceeds in the forward direction.
- (3R)-hydroxyoctanoyl-CoA + NAD+ = 3-oxooctanoyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
- (3R)-hydroxyhexadecanoyl-CoA + NAD+ = 3-oxohexadecanoyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
- (2E)-hexadecenedioyl-CoA + H2O = (3R)-hydroxyhexadecanedioyl-CoAThis reaction proceeds in the forward direction.
- (3R)-hydroxyhexadecanedioyl-CoA + NAD+ = 3-oxohexadecanedioyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
- (3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2OThis reaction proceeds in the backward direction.
- (3R)-3-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2OThis reaction proceeds in the backward direction.
- (3R)-3-hydroxydecanoyl-CoA + NAD+ = 3-oxodecanoyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
- (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + NAD+ = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + H+ + NADHThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13-37 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LVTGAGGGLGRAYALAFAERGALVI | ||||||
Binding site | 21 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 40 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 75-76 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SV | ||||||
Binding site | 99 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 151 | substrate | ||||
Sequence: S | ||||||
Active site | 164 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 164-168 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: YSAAK | ||||||
Binding site | 196-199 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AGSR | ||||||
Binding site | 405-406 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: HG | ||||||
Binding site | 434 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 509-514 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: DWNPLH | ||||||
Binding site | 532 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 562 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 705 | substrate | ||||
Sequence: Q | ||||||
Binding site | 723 | substrate | ||||
Sequence: Q |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal multifunctional enzyme type 2
- Short namesMFE-2
- Alternative names
- Cleaved into 2 chains
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 accessionP51660
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 30 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000400084 | 1-311 | (3R)-hydroxyacyl-CoA dehydrogenase | |||
Sequence: MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVIVNDLGGDFKGIGKGSSAADKVVAEIRRKGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIHRVHLRGSFQVTRAAWDHMKKQNYGRILMTSSASGIYGNFGQANYSAAKLGILGLCNTLAIEGRKNNIHCNTIAPNAGSRMTETVLPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWEKICDFSNASKPQTIQESTGGIVEVLHKVDSEGISPNR | ||||||
Chain | PRO_0000054584 | 1-735 | Peroxisomal multifunctional enzyme type 2 | |||
Sequence: MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVIVNDLGGDFKGIGKGSSAADKVVAEIRRKGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIHRVHLRGSFQVTRAAWDHMKKQNYGRILMTSSASGIYGNFGQANYSAAKLGILGLCNTLAIEGRKNNIHCNTIAPNAGSRMTETVLPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWEKICDFSNASKPQTIQESTGGIVEVLHKVDSEGISPNRTSHAAPAATSGFVGAVGHKLPSFSSSYTELQSIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSMMNGGLAEVPGLSFNFAKALHGEQYLELYKPLPRSGELKCEAVIADILDKGSGVVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISNAYVDLVPASGVSTQTPSEGGELQSALVFGEIGRRLKSVGREVVKKANAVFEWHITKGGTVAAKWTIDLKSGSGEVYQGPAKGSADVTIIISDEDFMEVVFGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL | ||||||
Modified residue | 46 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 46 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 52 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 57 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 68 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 84 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 265 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 275 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 304 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 308 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000400085 | 312-735 | Enoyl-CoA hydratase 2 | |||
Sequence: TSHAAPAATSGFVGAVGHKLPSFSSSYTELQSIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSMMNGGLAEVPGLSFNFAKALHGEQYLELYKPLPRSGELKCEAVIADILDKGSGVVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISNAYVDLVPASGVSTQTPSEGGELQSALVFGEIGRRLKSVGREVVKKANAVFEWHITKGGTVAAKWTIDLKSGSGEVYQGPAKGSADVTIIISDEDFMEVVFGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL | ||||||
Modified residue | 355 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 423 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 564 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 578 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 662 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 668 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 706 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 724 | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Present in many tissues with highest concentrations in liver and kidney.
Gene expression databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P51660 | HTT P42858 | 15 | EBI-8328056, EBI-466029 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-305 | (3R)-hydroxyacyl-CoA dehydrogenase | ||||
Sequence: MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVIVNDLGGDFKGIGKGSSAADKVVAEIRRKGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIHRVHLRGSFQVTRAAWDHMKKQNYGRILMTSSASGIYGNFGQANYSAAKLGILGLCNTLAIEGRKNNIHCNTIAPNAGSRMTETVLPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWEKICDFSNASKPQTIQESTGGIVEVLHKVDSE | ||||||
Region | 321-621 | Enoyl-CoA hydratase 2 | ||||
Sequence: SGFVGAVGHKLPSFSSSYTELQSIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSMMNGGLAEVPGLSFNFAKALHGEQYLELYKPLPRSGELKCEAVIADILDKGSGVVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISNAYVDLVPASGVSTQTPSEGGEL | ||||||
Domain | 483-599 | MaoC-like | ||||
Sequence: VPNRPPDAVLRDATSLNQAALYRLSGDWNPLHIDPDFASVAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVHETGDVVISN | ||||||
Domain | 623-735 | SCP2 | ||||
Sequence: SALVFGEIGRRLKSVGREVVKKANAVFEWHITKGGTVAAKWTIDLKSGSGEVYQGPAKGSADVTIIISDEDFMEVVFGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL | ||||||
Motif | 733-735 | Microbody targeting signal | ||||
Sequence: AKL |
Sequence similarities
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length735
- Mass (Da)79,482
- Last updated2007-01-23 v3
- ChecksumAD7804FE93EB9BA8
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 17 | in Ref. 1; CAA62015 | ||||
Sequence: A → P | ||||||
Sequence conflict | 417 | in Ref. 1; CAA62015 | ||||
Sequence: P → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X89998 EMBL· GenBank· DDBJ | CAA62015.1 EMBL· GenBank· DDBJ | mRNA | ||
AK004866 EMBL· GenBank· DDBJ | BAB23627.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088381 EMBL· GenBank· DDBJ | BAC40317.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166801 EMBL· GenBank· DDBJ | BAE39029.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167060 EMBL· GenBank· DDBJ | BAE39222.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169077 EMBL· GenBank· DDBJ | BAE40862.1 EMBL· GenBank· DDBJ | mRNA | ||
BC022175 EMBL· GenBank· DDBJ | AAH22175.1 EMBL· GenBank· DDBJ | mRNA |