Q3JAC1
Gene name |
lpxB |
Protein name |
Lipid-A-disaccharide synthase |
Names |
|
Species |
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107) |
KEGG Pathway |
noc:Noc_1753 |
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 Q3JAC1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3JAC1-F1 | Predicted | AlphaFoldDB |
No variants for Q3JAC1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3JAC1 | |||||
No associated diseases with Q3JAC1
No regional properties for Q3JAC1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q3JAC1 | |||
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 |
| MENSAPLVAI | VAGEASGDQH | AAHLIREVKK | IAPGVRFGGI | AGPQMRAAGV | EPLFDSSRLA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVGLVEVLSH | LNEIYGAMQK | MRHFLEEKHP | DLLILVDYPE | FNLRLAKRAK | TLGIKVLYYI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SPQVWAWRQY | RVHQIGQVVD | MMAVVLPFEV | PFYEQAGVPV | NFVGHPLQHE | VKSKFNRNEA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVEFGFNPCC | KTLGLLPGSR | HSEIKRLLPV | LLEAAERIYS | EEPEIQYLLP | LAATLKEIDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| APYLKGYRLP | LRVIPDRSYD | VMAACDAMVA | ASGTVTLEAA | LMGVPLVVIY | KMNSLSYWMG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RLLIKVDHIA | LCNIIAGEGV | APELIQQDAS | PERIALEALN | LLRDKERRQT | MQQKFYAIKH |
| 370 | 380 | ||||
| KLGAGAQRTI | AELTVAMLEG | ENLGRAS |