C3LSH8
Gene name |
add |
Protein name |
Adenosine deaminase |
Names |
Adenosine aminohydrolase |
Species |
Vibrio cholerae serotype O1 (strain M66-2) |
KEGG Pathway |
vcm:VCM66_2671 |
EC number |
3.5.4.4: In cyclic amidines |
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 C3LSH8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C3LSH8-F1 | Predicted | AlphaFoldDB |
No variants for C3LSH8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C3LSH8 | |||||
No associated diseases with C3LSH8
1 regional properties for C3LSH8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Adenosine deaminase domain | 7 - 329 | IPR001365 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.4.4 | In cyclic amidines |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2'-deoxyadenosine deaminase activity | Catalysis of the reaction: 2'-deoxyadenosine + H2O = deoxyinosine + NH3. |
| adenosine deaminase activity | Catalysis of the reaction: adenosine + H2O = inosine + NH3. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| nucleotide metabolic process | The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates). |
| purine ribonucleoside monophosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of purine ribonucleoside monophosphate, a compound consisting of a purine base linked to a ribose sugar esterified with phosphate on the sugar. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MITSSLPLTD | LHRHLDGNIR | TQTILELGQK | FGVKLPANTL | QTLTPYVQIV | EAEPSLVAFL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SKLDWGVAVL | GDLDACRRVA | YENVEDALNA | RIDYAELRFS | PYYMAMKHSL | PVTGVVEAVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGVRAGVRDF | GIQANLIGIM | SRTFGTDACQ | QELDAILSQK | NHIVAVDLAG | DELGQPGDRF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IQHFKQVRDA | GLHVTVHAGE | AAGPESMWQA | IRDLGATRIG | HGVKAIHDPK | LMDYLAQHRI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIESCLTSNL | QTSTVDSLAT | HPLKRFLEHG | ILACINTDDP | AVEGIELPYE | YEVAAPQAGL |
| 310 | 320 | 330 | |||
| SQEQIRQAQL | NGLELAFLSD | SEKKALLAKA | ALRG |