P0AB89
Gene name |
purB (b1131, JW1117) |
Protein name |
Adenylosuccinate lyase |
Names |
ASL, Adenylosuccinase, ASase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b1131 |
EC number |
4.3.2.2: Lyases acting on amides, amidines, etc |
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
4 structures for P0AB89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2PTQ | X-ray | 200 A | A/B | 1-456 | PDB |
| 2PTR | X-ray | 185 A | A/B | 1-456 | PDB |
| 2PTS | X-ray | 200 A | A | 1-456 | PDB |
| AF-P0AB89-F1 | Predicted | AlphaFoldDB |
No variants for P0AB89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0AB89 | |||||
No associated diseases with P0AB89
Functions
| Description | ||
|---|---|---|
| EC Number | 4.3.2.2 | Lyases acting on amides, amidines, etc |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity | Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. |
| guanosine tetraphosphate binding | Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions. |
| N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity | Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' AMP biosynthetic process | The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP). |
| 'de novo' IMP biosynthetic process | The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MELSSLTAVS | PVDGRYGDKV | SALRGIFSEY | GLLKFRVQVE | VRWLQKLAAH | AAIKEVPAFA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADAIGYLDAI | VASFSEEDAA | RIKTIERTTN | HDVKAVEYFL | KEKVAEIPEL | HAVSEFIHFA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CTSEDINNLS | HALMLKTARD | EVILPYWRQL | IDGIKDLAVQ | YRDIPLLSRT | HGQPATPSTI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GKEMANVAYR | MERQYRQLNQ | VEILGKINGA | VGNYNAHIAA | YPEVDWHQFS | EEFVTSLGIQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WNPYTTQIEP | HDYIAELFDC | VARFNTILID | FDRDVWGYIA | LNHFKQKTIA | GEIGSSTMPH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVNPIDFENS | EGNLGLSNAV | LQHLASKLPV | SRWQRDLTDS | TVLRNLGVGI | GYALIAYQST |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LKGVSKLEVN | RDHLLDELDH | NWEVLAEPIQ | TVMRRYGIEK | PYEKLKELTR | GKRVDAEGMK |
| 430 | 440 | 450 | |||
| QFIDGLALPE | EEKARLKAMT | PANYIGRAIT | MVDELK |