Q7VXJ5
Gene name |
dapE |
Protein name |
Succinyl-diaminopimelate desuccinylase |
Names |
SDAP desuccinylase, N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase |
Species |
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) |
KEGG Pathway |
bpe:BP1763 |
EC number |
3.5.1.18: In linear amides |
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 Q7VXJ5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7VXJ5-F1 | Predicted | AlphaFoldDB |
No variants for Q7VXJ5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7VXJ5 | |||||
No associated diseases with Q7VXJ5
1 regional properties for Q7VXJ5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M20, dimerisation domain | 177 - 284 | IPR011650 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.1.18 | In linear amides |
| 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 |
|---|---|
| cobalt ion binding | Binding to a cobalt ion (Co). |
| succinyl-diaminopimelate desuccinylase activity | Catalysis of the reaction: N-succinyl-LL-2,6-diaminopimelate + H(2)O = LL-2,6-diaminopimelate + succinate. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| diaminopimelate biosynthetic process | The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls. |
| lysine biosynthetic process via diaminopimelate | The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTASAVLDLV | KDLIARPSVT | PDDVDCQMLL | AQRLERIGFQ | CETIARGGVT | NLWARRGAGA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PLTVFAGHTD | VVPPGPRDKW | DSDPFVPTER | DGFLYGRGAA | DMKSSIAAFV | VAAEEFVAVH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PEHPGSIALL | ITSDEEGPAV | DGTVIVCDEL | RQRGEQLDYC | IVGEPTSTEA | LGDVCKNGRR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSLSGRLLVK | GVQGHVAYPH | LARNPVHQLA | PALTELVAIE | WDQGNEYFPP | TTFQVSNLHA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GTGATNVVPG | EAVALFNFRF | STASTPGQLK | ARVHEVLDRH | GLEYQLDWEL | GGEPFLTPRG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLTDALVSAI | QAETGLQAEL | STTGGTSDGR | FIARICPQVI | EFGPCNATIH | KVNERIELSS |
| 370 | |||||
| LAPLKNIYRR | TLENLLLAD |