B9JEX8
Gene name |
lpxD |
Protein name |
UDP-3-O-acylglucosamine N-acyltransferase |
Names |
|
Species |
Agrobacterium radiobacter (strain K84 / ATCC BAA-868) |
KEGG Pathway |
ara:Arad_2229 |
EC number |
2.3.1.191: Transferring groups other than amino-acyl groups |
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 B9JEX8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B9JEX8-F1 | Predicted | AlphaFoldDB |
No variants for B9JEX8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B9JEX8 | |||||
No associated diseases with B9JEX8
4 regional properties for B9JEX8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Hexapeptide repeat | 148 - 180 | IPR001451-1 |
| repeat | Hexapeptide repeat | 241 - 276 | IPR001451-2 |
| conserved_site | Hexapeptide transferase, conserved site | 286 - 314 | IPR018357 |
| domain | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region | 35 - 99 | IPR020573 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.191 | Transferring groups other than amino-acyl groups |
| 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 |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| N-acyltransferase activity | Catalysis of the transfer of an acyl group to a nitrogen atom on the acceptor molecule. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| lipid A biosynthetic process | The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEHIGFFPPH | DGVSLRALAE | HLGAELADEA | FAGVIIKSIA | PVYRAGDGDV | CYLLSRKNRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELETCKASAI | ICLPTLSSLV | PEHIPVLLSK | KPHTDFALAG | ALLHPQAMRP | VALTSTPTLI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SPTAFVDPTA | KLEADVGVEP | GAVVGPGAEI | GEGTRIGAGA | IIGPGVKIGR | HCTIGGGASV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LCSYLGNGVI | IHNGARIGQD | GFGYAPSPRG | MIKIVQIGRV | IIQDNVEIGA | NTTIDRGTMD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DTVIGEGTKI | DNQVQIGHNV | RIGRYCAIVS | QVGIAGSAVI | GDGVQIGGHT | GINGHIQIGD |
| 310 | 320 | 330 | 340 | 350 | |
| GVQIGAMSGV | MNSIPAGERF | AGIPARPLWD | FLREAAEVAK | RSGAREKKDG | SAEHD |