Q5RAT4
Gene name |
ENOSF1 |
Protein name |
Mitochondrial enolase superfamily member 1 |
Names |
L-fuconate dehydratase |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100172579 |
EC number |
4.2.1.68: Hydro-lyases |
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
1 structures for Q5RAT4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RAT4-F1 | Predicted | AlphaFoldDB |
No variants for Q5RAT4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RAT4 | |||||
No associated diseases with Q5RAT4
4 regional properties for Q5RAT4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Mandelate racemase/muconate lactonizing enzyme, N-terminal domain | 35 - 138 | IPR013341 |
| domain | Mandelate racemase/muconate lactonizing enzyme, C-terminal | 201 - 296 | IPR013342 |
| conserved_site | Mandelate racemase/muconate lactonizing enzyme, conserved site | 247 - 278 | IPR018110 |
| domain | Enolase C-terminal domain-like | 206 - 421 | IPR029065 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.68 | Hydro-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| isomerase activity | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. |
| L-fuconate dehydratase activity | Catalysis of the reaction: L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H(2)O. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular amino acid catabolic process | The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents. |
| cellular carbohydrate catabolic process | The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, as carried out by individual cells. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVRGRIFRLS | VRDVRFPTSL | GGHGSDAMHT | DPDYSAAYVV | IETDAEDGIK | GCGITFTLGK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GTEVVVCAVN | ALAHHVLNKD | LKDIVGDFRG | FYRQLTSDGQ | PRWIGPEKGV | VHLATAAVLN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVWDLWAKQE | GKPVWKLLVD | MDPRTLVSCI | DFRYITDVLT | EEDALEILQK | GQVGKKEREK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QMLAQGYPAY | TTSCAWLGYS | DDTLKQLCAQ | ALKDGWTRFK | VKVGADLQDD | VRRCQIIRDM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGLEKTLMMD | ANQRWDVPEA | VEWMSKLAKF | KPLWIEEPTS | PDDILGHATI | SKALVPLGIG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IATGEQCHNR | VIFKQLLQAK | ALQFLQIDSC | RLGSVNENLS | VLLMAKKFEI | PVCPHAGGVG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LCELVQHLII | FDYISVSASL | ENRMCEYVDH | LHEHFKYPVM | IQRASYMPPK | DPGYSTEMKE |
| 430 | 440 | ||||
| ESVKKHQYPD | GEVWKKLLAA | QEN |