A4VWC5
Gene name |
deoB |
Protein name |
Phosphopentomutase |
Names |
Phosphodeoxyribomutase |
Species |
Streptococcus suis (strain 05ZYH33) |
KEGG Pathway |
ssu:SSU05_1448 |
EC number |
5.4.2.7: Phosphotransferases (phosphomutases) |
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 A4VWC5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4VWC5-F1 | Predicted | AlphaFoldDB |
No variants for A4VWC5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4VWC5 | |||||
No associated diseases with A4VWC5
5 regional properties for A4VWC5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | 94 - 105 | IPR000291-1 |
| conserved_site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | 279 - 307 | IPR000291-2 |
| domain | D-alanine--D-alanine ligase, C-terminal | 135 - 333 | IPR011095 |
| domain | D-alanine--D-alanine ligase, N-terminal domain | 6 - 116 | IPR011127 |
| domain | ATP-grasp fold | 132 - 334 | IPR011761 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.4.2.7 | Phosphotransferases (phosphomutases) |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| phosphopentomutase activity | Catalysis of the reaction: D-ribose 1-phosphate = D-ribose 5-phosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| 5-phosphoribose 1-diphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate. |
| cellular metabolic compound salvage | Any process which produces a useful metabolic compound from derivatives of it without de novo synthesis, as carried out by individual cells. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPKFKRVHLV | VMDSVGIGAA | PDSDKFFNAG | VADTESDTLG | HISEKAGLEV | PNMTKIGLGN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IPRDTALATV | PAESHPTGYV | TKLEEVSLGK | DTMTGHWEIM | GLNITEPFDT | FWDGFPEEIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TKIEEFSGRK | IIREANKPYS | GTAVIDDFGP | RQMETGELIV | YTSADPVLQI | AAHEDIIPLD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELYRICEYAR | SITLERPALL | GRIIARPYVG | EPGNFSRTAN | RHDYAVSPFE | ATVLNKLADA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVPTYSVGKI | SDIFNGSGIT | NDMGHTKSNM | HGVDVLIDTL | KLSDFEEGFS | FTNLVDFDAV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YGHRRNIEGY | RDCLQEFDAR | IPEIIDNMRE | DDLLLITADH | GNDPSYAGTD | HTREYVPLLA |
| 370 | 380 | 390 | 400 | ||
| YSKAFKGSGV | LPVGHFADIS | ATVAENFGVD | TAMIGESFLS | QLV |