Q9VXJ0 · DHB4_DROME
- ProteinPeroxisomal multifunctional enzyme type 2
- GeneMfe2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids598 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids.
Miscellaneous
Complements functionally the S.cerevisiae peroxisomal MFE-2 in vivo.
Catalytic activity
- a (3R)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + H+ + NADH
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
85.3 μM | (2E)-butenoyl-CoA | 22 | ||||
66.7 μM | (2E)-hexenoyl-CoA | 22 | ||||
31.4 μM | (2E)-decenoyl-CoA | 22 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.07 μmol/min/mg | 22 | with (2E)-butenoyl-CoA | |||
15 μmol/min/mg | 22 | with (2E)-hexenoyl-CoA | |||
31.4 μmol/min/mg | 22 | with (2E)-decenoyl-CoA |
Catalytic efficiency is similar using full-length protein or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase 2 domains in a 1:1 mixture.
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16-40 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VVTGAGAGLGREYALLFAERGAKVV | ||||||
Binding site | 24 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 43 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 78-79 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SV | ||||||
Binding site | 102 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 154 | substrate | ||||
Sequence: S | ||||||
Active site | 167 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 167-171 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: YTAAK | ||||||
Binding site | 199-202 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AASR | ||||||
Binding site | 390-391 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: HG | ||||||
Binding site | 419 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 496-501 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: DKNPLH | ||||||
Binding site | 519 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 549 | (3R)-3-hydroxydecanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: F |
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 dehydratase activity | |
Molecular Function | 3-hydroxyacyl-CoA dehydrogenase activity | |
Molecular Function | enoyl-CoA hydratase activity | |
Molecular Function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid beta-oxidation using acyl-CoA oxidase |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisomal multifunctional enzyme type 2
- Short namesDmMFE-2
Including 2 domains:
- Recommended name(3R)-hydroxyacyl-CoA dehydrogenase
- EC number
- Recommended nameEnoyl-CoA hydratase 2
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VXJ0
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416935 | 1-598 | Peroxisomal multifunctional enzyme type 2 | |||
Sequence: MSSSDGKLRYDGRVAVVTGAGAGLGREYALLFAERGAKVVVNDLGGTHSGDGASQRAADIVVDEIRKAGGEAVADYNSVIDGAKVIETAIKAFGRVDILVNNAGILRDRSLVKTSEQDWNLVNDVHLKGSFKCTQAAFPYMKKQNYGRIIMTSSNSGIYGNFGQVNYTAAKMGLIGLANTVAIEGARNNVLCNVIVPTAASRMTEGILPDILFNELKPKLIAPVVAYLCHESCEDNGSYIESAAGWATKLHMVRGKGAVLRPSLDDPVTIEYVKDVWSNVTDMSKAKHLGAIAEASGTLLEVLEKLKEGGGDAIEDAFEFNSKELITYALGIGASVKNAKDMRFLYENDADFAAIPTFFVLPGLLLQMSTDKLLSKALPNSQVDFSNILHGEQYLEIVDDLPTSGTLLTNGKVFDVMDKGSGAVVVTNSESFDESGRLLVRNQSTTFIVGAGKFGGKKDPIAGVVPLQPAPNRQPDATVQYTTSEDQAALYRLSGDKNPLHIDPQMALLAGFKTPILHGLCTLGFSVRAVLAQFADNNPALFKAVKVRFSGPVIPGQTLRVDLWKQGTRINFRTVVVETGKEVISGAYVDLKSSQAKL |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-309 | (3R)-hydroxyacyl-CoA dehydrogenase | ||||
Sequence: MSSSDGKLRYDGRVAVVTGAGAGLGREYALLFAERGAKVVVNDLGGTHSGDGASQRAADIVVDEIRKAGGEAVADYNSVIDGAKVIETAIKAFGRVDILVNNAGILRDRSLVKTSEQDWNLVNDVHLKGSFKCTQAAFPYMKKQNYGRIIMTSSNSGIYGNFGQVNYTAAKMGLIGLANTVAIEGARNNVLCNVIVPTAASRMTEGILPDILFNELKPKLIAPVVAYLCHESCEDNGSYIESAAGWATKLHMVRGKGAVLRPSLDDPVTIEYVKDVWSNVTDMSKAKHLGAIAEASGTLLEVLEKLKEG | ||||||
Region | 310-598 | Enoyl-CoA hydratase 2 | ||||
Sequence: GGDAIEDAFEFNSKELITYALGIGASVKNAKDMRFLYENDADFAAIPTFFVLPGLLLQMSTDKLLSKALPNSQVDFSNILHGEQYLEIVDDLPTSGTLLTNGKVFDVMDKGSGAVVVTNSESFDESGRLLVRNQSTTFIVGAGKFGGKKDPIAGVVPLQPAPNRQPDATVQYTTSEDQAALYRLSGDKNPLHIDPQMALLAGFKTPILHGLCTLGFSVRAVLAQFADNNPALFKAVKVRFSGPVIPGQTLRVDLWKQGTRINFRTVVVETGKEVISGAYVDLKSSQAKL | ||||||
Domain | 469-586 | MaoC-like | ||||
Sequence: PAPNRQPDATVQYTTSEDQAALYRLSGDKNPLHIDPQMALLAGFKTPILHGLCTLGFSVRAVLAQFADNNPALFKAVKVRFSGPVIPGQTLRVDLWKQGTRINFRTVVVETGKEVISG | ||||||
Motif | 596-598 | 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
- Length598
- Mass (Da)64,073
- Last updated2000-05-01 v1
- Checksum24205DE78964319A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
X2JFD6 | X2JFD6_DROME | Mfe2 | 598 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014298 EMBL· GenBank· DDBJ | AAF48572.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051493 EMBL· GenBank· DDBJ | AAK92917.1 EMBL· GenBank· DDBJ | mRNA |