B5YGX0
Gene name |
glmM |
Protein name |
Phosphoglucosamine mutase |
Names |
|
Species |
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87) |
KEGG Pathway |
tye:THEYE_A0046 |
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 B5YGX0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5YGX0-F1 | Predicted | AlphaFoldDB |
No variants for B5YGX0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5YGX0 | |||||
No associated diseases with B5YGX0
5 regional properties for B5YGX0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Alpha-D-phosphohexomutase, C-terminal | 392 - 443 | IPR005843 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain I | 2 - 137 | IPR005844 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain II | 159 - 256 | IPR005845 |
| domain | Alpha-D-phosphohexomutase, alpha/beta/alpha domain III | 260 - 370 | IPR005846 |
| conserved_site | Alpha-D-phosphohexomutase, conserved site | 95 - 104 | IPR016066 |
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 | |
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 |
|---|---|
| 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. |
| phosphomannomutase activity | Catalysis of the reaction: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. |
3 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. |
| peptidoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls. |
| UDP-N-acetylglucosamine biosynthetic process | The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRIFGTDGIR | GTINNYPMTP | EVCLRAGMAL | CFLLKKRLPH | KPKILIGKDT | RISGYVIESA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTSGITSMGG | DVYLVGPIPT | PAVAFLVKSM | RVDAGIVISA | SHNPFSDNGI | KIFSNDGFKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TEELENDIEK | LINDKDFPAI | RPSARELGKA | YRIEDAQGRY | IEFIKSTLPK | DSNLEGLKVA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IDPANGAAYK | ITPTLFHELG | AEVITINDKP | DGVNINKECG | ALYPESLIKI | VKETQAHFGV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AHDGDADRTI | LVDEKGNIVD | GDFILTILAE | ELKKERKLKK | NTVVATIMTN | MGVENYLKNA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GIKMIRTKVG | DKYVVEEMLK | GGYNLGGEQS | GHIICMDYTN | TGDGPITAVQ | MAYIIKKNQF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLSELIKNIP | RYPQALKNIK | IPEKLPKDEV | KNVIKKLSQK | ASTLEKNMRG | RIIIRPSGTE |
| 430 | 440 | 450 | |||
| PKIRIMVEDE | NPERLKQVLD | ELEAVANMML | S |