P23965
Gene name |
Eci1 |
Protein name |
Enoyl-CoA delta isomerase 1, mitochondrial |
Names |
MECI, 3,2-trans-enoyl-CoA isomerase, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
|
EC number |
5.3.3.8: Transposing C=C bonds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for P23965
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1XX4 | X-ray | 220 A | A | 29-289 | PDB |
| AF-P23965-F1 | Predicted | AlphaFoldDB |
No variants for P23965
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P23965 | |||||
No associated diseases with P23965
1 regional properties for P23965
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Enoyl-CoA hydratase/isomerase, conserved site | 130 - 150 | IPR018376 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.3.3.8 | Transposing C=C bonds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| delta(3)-delta(2)-enoyl-CoA isomerase activity | Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA. |
| enoyl-CoA hydratase activity | Catalysis of the reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O. |
| identical protein binding | Binding to an identical protein or proteins. |
| intramolecular oxidoreductase activity, transposing C=C bonds | Catalysis of an oxidation-reduction (redox) reaction in which the hydrogen donor and acceptor are the same molecule, one or more carbon-carbon double bonds in the molecule are rearranged, and no oxidized product appears. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q39659 | Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a | Cucumis sativus (Cucumber) | PR | |
| Q08426 | EHHADH | Peroxisomal bifunctional enzyme | Homo sapiens (Human) | PR |
| P42126 | ECI1 | Enoyl-CoA delta isomerase 1, mitochondrial | Homo sapiens (Human) | PR |
| Q8W1L6 | MFP | Peroxisomal fatty acid beta-oxidation multifunctional protein | Oryza sativa subsp japonica (Rice) | PR |
| Q9ZPI5 | MFP2 | Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALAAARRVL | LQAGSRLGRR | GAVDGARRFS | NKRVLVEKEG | EAGIAVMKFK | NPPVNSLSLE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLTEFVISLE | KLENDKSIRG | VILTSERPGI | FSAGLDLMEM | YGRNPAHYAE | YWKAVQELWL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RLYLSNLTLI | SAINGASPAG | GCLMALTCDY | RIMADNSKYT | IGLNESLLGI | VAPFWLKDNY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VNTIGHRAAE | RALQLGTLFP | PAEALKVGLV | DEVVPEDQVH | SKARSVMAKW | FTIPDHSRQL |
| 250 | 260 | 270 | 280 | ||
| TKSMMRKATA | DNLIKQREAD | IQNFTSFISR | DSIQKSLHVY | LEKLKQKKG |