A1K6Q8
Gene name |
lpxB |
Protein name |
Lipid-A-disaccharide synthase |
Names |
|
Species |
Azoarcus sp (strain BH72) |
KEGG Pathway |
azo:azo1896 |
EC number |
2.4.1.182: 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 A1K6Q8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1K6Q8-F1 | Predicted | AlphaFoldDB |
No variants for A1K6Q8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1K6Q8 | |||||
No associated diseases with A1K6Q8
No regional properties for A1K6Q8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A1K6Q8 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.182 | 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 |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| lipid-A-disaccharide synthase activity | Catalysis of the reaction: 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + UDP-2,3-bis(3-hydroxytetradecanoyl)-D-glucosamine = 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + H(+) + UDP. |
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 |
| MAPRIAMVAG | EASGDLLASH | LIRAIRARVP | DAEFFGIGGP | KMQAEGFDAR | WPCELLAVHG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YVDALKRYRE | LSGIRKKLLK | QVRRERPDAF | IGVDAPDFNL | WLEGKIKAAG | IPAIHFVSPS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IWAWRGGRIK | RIARSVTRML | CMFPFEPELY | ERAGVPVSYV | GHPLADVFPL | EPDRAAARER |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LDIAPERKVV | ALLPGSRQSE | VRNLGELFIE | TAAMLAQRHP | DVLFLVPLAT | RETRELFSAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LARNKGDELP | LRMLFGHAVD | AMTAADAVLV | ASGTASLEAA | LLKRPMVITY | RMGKWQYRLM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KRMAYLPWIG | LPNILCREGL | VPELVQDDAT | PPKLADALER | WLVDPAACAA | LTERFTALHH |
| 370 | 380 | 390 | |||
| SLRQNTAEKA | AAAVLPYLSS | SASCQPVSVS | A |