Q8FSH1
Gene name |
mshA |
Protein name |
D-inositol 3-phosphate glycosyltransferase |
Names |
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase, GlcNAc-Ins-P N-acetylglucosaminyltransferase |
Species |
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) |
KEGG Pathway |
cef:CE0422 |
EC number |
2.4.1.250: Hexosyltransferases |
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 Q8FSH1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8FSH1-F1 | Predicted | AlphaFoldDB |
No variants for Q8FSH1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8FSH1 | |||||
No associated diseases with Q8FSH1
1 regional properties for Q8FSH1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Large-conductance mechanosensitive channel, conserved site | 11 - 24 | IPR019823 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.250 | Hexosyltransferases |
| 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 |
|---|---|
| acetylglucosaminyltransferase activity | Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar. |
| D-inositol-3-phosphate glycosyltransferase activity | Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + 1D-myo-inositol 3-phosphate = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + UDP + H+. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| mycothiol biosynthetic process | The chemical reactions and pathways resulting in the formation of mycothiol, which consists of N-acetyl-L-cysteine linked to a pseudodisaccharide, D-glucosamine and myo-inositol. Mycothiol is produced in actinomycetes like mycobacteria and serves similar functions to glutathione. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRVAMISMHT | SPLQQPGVGD | SGGMNVYILS | TGTELARQGV | EVDIFTRATR | PSQGEVVQVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNLRVINIVA | GPYEGLAKEE | LSTQLAAFAG | GVLEFTRRGG | IEYDLIHSHY | WLSGQVGWLM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDLWRIPLVH | TAHTLAAVKN | SYRADEDTPE | SEARRICEQQ | LVDNADVLAV | NTQEELADLV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HHYDADPDRI | SVVSPGADIA | LYTPGNDRAT | ERSRRELGVP | LHAKVVAFVG | RLQPFKGPQV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LIHAVAELLE | RDPQRNLRVL | ICGGPSGPSA | TPETYRNLAV | ELGVDKRIRF | LDPRPPEELV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVYRAADIIA | VPSYNESFGL | VAMEAQATGT | PVVAARVGGL | PVAVAEGETG | LLVDGHDPAL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WADTLATLLD | DDETRIRMGQ | DAVEHARNFS | WAATATQLSS | LYSEATTAEC | DGGIPRRADG |
| ARWD |