P0A6L0
Gene name |
deoC |
Protein name |
Deoxyribose-phosphate aldolase |
Names |
DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b4381 |
EC number |
4.1.2.4: Aldehyde-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
12 structures for P0A6L0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1JCJ | X-ray | 110 A | A/B | 1-259 | PDB |
| 1JCL | X-ray | 105 A | A/B | 1-259 | PDB |
| 1KTN | X-ray | 140 A | A/B | 1-250 | PDB |
| 1P1X | X-ray | 099 A | A/B | 1-259 | PDB |
| 5EKY | X-ray | 110 A | A | 1-259 | PDB |
| 5EL1 | X-ray | 125 A | A | 1-259 | PDB |
| 5EMU | X-ray | 150 A | A | 1-259 | PDB |
| 6Z9H | X-ray | 172 A | A/B | 2-259 | PDB |
| 6Z9I | X-ray | 186 A | A/B | 1-250 | PDB |
| 6Z9J | X-ray | 150 A | A/B | 1-250 | PDB |
| 7P75 | X-ray | 123 A | AAA/BBB | 1-259 | PDB |
| AF-P0A6L0-F1 | Predicted | AlphaFoldDB |
No variants for P0A6L0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0A6L0 | |||||
No associated diseases with P0A6L0
No regional properties for P0A6L0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P0A6L0 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.2.4 | Aldehyde-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| deoxyribose-phosphate aldolase activity | Catalysis of the reaction: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. |
| lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| cellular response to DNA damage stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| deoxyribonucleotide catabolic process | The chemical reactions and pathways resulting in the breakdown of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. |
| deoxyribose phosphate catabolic process | The chemical reactions and pathways resulting in the breakdown of deoxyribose phosphate, the phosphorylated sugar 2-deoxy-erythro-pentose. |
| nucleobase-containing small molecule interconversion | The chemical reactions and pathways by which a nucleobase, nucleoside or nucleotide small molecule is synthesized from another nucleobase, nucleoside or nucleotide small molecule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDLKASSLR | ALKLMDLTTL | NDDDTDEKVI | ALCHQAKTPV | GNTAAICIYP | RFIPIARKTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEQGTPEIRI | ATVTNFPHGN | DDIDIALAET | RAAIAYGADE | VDVVFPYRAL | MAGNEQVGFD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVKACKEACA | AANVLLKVII | ETGELKDEAL | IRKASEISIK | AGADFIKTST | GKVAVNATPE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SARIMMEVIR | DMGVEKTVGF | KPAGGVRTAE | DAQKYLAIAD | ELFGADWADA | RHYRFGASSL |
| 250 | |||||
| LASLLKALGH | GDGKSASSY |