A7Z0V3
Gene name |
glmM |
Protein name |
Phosphoglucosamine mutase |
Names |
|
Species |
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) |
KEGG Pathway |
bay:RBAM_002300 |
EC number |
5.4.2.10: 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 A7Z0V3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7Z0V3-F1 | Predicted | AlphaFoldDB |
No variants for A7Z0V3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A7Z0V3 | |||||
No associated diseases with A7Z0V3
Functions
| Description | ||
|---|---|---|
| EC Number | 5.4.2.10 | Phosphotransferases (phosphomutases) |
| 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phosphoglucosamine mutase activity | Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGKYFGTDGV | RGVANSELTP | ELAFKVGRFG | GYVLTKDKQR | PKVLIGRDTR | ISGHMLEGAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VAGLLSIGAE | VMRLGVISTP | GVSYLTKAMD | AEAGVMISAS | HNPVQDNGIK | FFGGDGFKLS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DEQEAEIERL | MDEPEDKLPR | PTGADLGLVN | DYFEGVQKYL | QFLKQTADED | FTGIHVALDC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AHGATSSIAT | HLFADLDADV | STMGTSPNGL | NINDGVGSTH | PEALSAFVKE | KNADIGLAFD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GDGDRLIAVD | EKGNIVDGDQ | IMYICAKYLK | SEGRLKDDTV | VSTVMSNLGF | YKALEKEEIK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVQTAVGDRY | VVEAMKKDGY | NVGGEQSGHL | IFLDYNTTGD | GLLSAIMLVN | TLKASGKTLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ELADEMKKFP | QLLVNVKVTD | KYKVEENAKV | KAVISEVEKE | MNGDGRILVR | PSGTEPLVRV |
| 430 | 440 | ||||
| MAEARTKELC | DEYVTKIVDV | VRTEMGAE |