Q01373 · FOX2_NEUCR
- ProteinPeroxisomal hydratase-dehydrogenase-epimerase
- Genefox-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids894 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
Catalytic activity
- a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 53 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 99 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 132 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 164 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 164 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 168 | Lowers pKa of active site Tyr | ||||
Sequence: K | ||||||
Binding site | 168 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 197 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 458 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 693 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 694 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 723 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 803 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 805 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 826 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 851 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 853 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity | |
Molecular Function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity | |
Molecular Function | 3-hydroxyacyl-CoA dehydrogenase activity | |
Molecular Function | enoyl-CoA hydratase activity | |
Molecular Function | isomerase activity | |
Biological Process | fatty acid beta-oxidation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal hydratase-dehydrogenase-epimerase
- Short namesHDE
- Alternative names
Including 2 domains:
- Recommended name2-enoyl-CoA hydratase
- EC number
- Recommended name(3R)-3-hydroxyacyl-CoA dehydrogenase
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora
Accessions
- Primary accessionQ01373
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Catalase-free microbodies.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054699 | 1-894 | Peroxisomal hydratase-dehydrogenase-epimerase | |||
Sequence: MAEQLRFDGQVVVVTGAGGGLGKAYCLFFGSRGASVVVNDLGASFKGEGNSTKAADVVVNEIKAAGGKAVANYDSVENGDKIIETAIKEFGRIDILINNAGILRDISFKNMKDEDWDLIFKVHVKGSYKTARAAWPYFRKQKFGRVINTASAAGLFGNFGQANYSAAKLGMVGFTETLAKEGLKYNIISNVIAPIAASRMTETVMPPDLLALMKPEWVVPLVAVLVHKNNTSETGSIFEVGGGHVAKLRWERSSGLLLKADESYTPGAIIKKWDQVTDFSNPQYPTGPNDFLALLEESLKLGPNDPGEKVDFKGRVALVTGGGAGIGRAYCLAFARAGASVVVNDLVNPDDVVNEIKKMGGKAVGAKFSAEDGDAVVKAAIDAFGRVDIVVNNAGILRDKAFHNMDDSLWDPVMNVHARGTYKVTKAAWPYFLKQKYGRVLNTTSTSGIYGNFGQANYSAAKCAILGFSRAIALEGAKYNIYVNTIAPNAGTAMTKTILPEELVQAFKPDYVAPLVLALCSDKVPKKPTGGLYEVGSGWCGQTRWQRSGGHGFPVDVPLTPEEVVKHWNDIVTFDSRADHPEKASDSIEKIMANMENRVGEGKSGAAENEHLAAIKKFTGVEGKGTEYTFTERDVCLYNLGIGAKRTDIKYIFEGNEDFEVVPTFGVIPPFNTEMPFSFDDIVPNFSPMMLLHGEQYLEVRKYPIPTSGRLVSKGKLLEVVDKGSAAIVKQGITTFNAETGEELFYNEMTVFLRGCGGFGGQKKPADRGASTAANKPPARSPDAVVEVQTTEEQAAIYRLSGDYNPLHVDPAFAKVGGFKVPILHGLCSFGIAGKAVYEKYGKFKNIKVRFAGTVNPGQTLVTEMWKEGNKVVFQTKVKETGKLAISGAAAELA |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 6-230 | Short-chain dehydrogenase like 1 | ||||
Sequence: RFDGQVVVVTGAGGGLGKAYCLFFGSRGASVVVNDLGASFKGEGNSTKAADVVVNEIKAAGGKAVANYDSVENGDKIIETAIKEFGRIDILINNAGILRDISFKNMKDEDWDLIFKVHVKGSYKTARAAWPYFRKQKFGRVINTASAAGLFGNFGQANYSAAKLGMVGFTETLAKEGLKYNIISNVIAPIAASRMTETVMPPDLLALMKPEWVVPLVAVLVHKNN | ||||||
Region | 311-523 | Short-chain dehydrogenase like 2 | ||||
Sequence: DFKGRVALVTGGGAGIGRAYCLAFARAGASVVVNDLVNPDDVVNEIKKMGGKAVGAKFSAEDGDAVVKAAIDAFGRVDIVVNNAGILRDKAFHNMDDSLWDPVMNVHARGTYKVTKAAWPYFLKQKYGRVLNTTSTSGIYGNFGQANYSAAKCAILGFSRAIALEGAKYNIYVNTIAPNAGTAMTKTILPEELVQAFKPDYVAPLVLALCSDK | ||||||
Region | 763-782 | Disordered | ||||
Sequence: KKPADRGASTAANKPPARSP | ||||||
Domain | 776-887 | MaoC-like | ||||
Sequence: KPPARSPDAVVEVQTTEEQAAIYRLSGDYNPLHVDPAFAKVGGFKVPILHGLCSFGIAGKAVYEKYGKFKNIKVRFAGTVNPGQTLVTEMWKEGNKVVFQTKVKETGKLAIS |
Domain
Contains two SDR domains.
Sequence similarities
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length894
- Mass (Da)96,326
- Last updated1996-11-01 v1
- Checksum29758220D397AA88
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X80052 EMBL· GenBank· DDBJ | CAA56355.1 EMBL· GenBank· DDBJ | mRNA | ||
CM002239 EMBL· GenBank· DDBJ | EAA32803.1 EMBL· GenBank· DDBJ | Genomic DNA |