B1XT16
Gene name |
lpxC |
Protein name |
UDP-3-O-acyl-N-acetylglucosamine deacetylase |
Names |
UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase |
Species |
Polynucleobacter necessarius subsp necessarius (strain STIR1) |
KEGG Pathway |
pne:Pnec_0188 |
EC number |
3.5.1.108: In linear amides |
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 B1XT16
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1XT16-F1 | Predicted | AlphaFoldDB |
No variants for B1XT16
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1XT16 | |||||
No associated diseases with B1XT16
No regional properties for B1XT16
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for B1XT16 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.1.108 | In linear amides |
| 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 |
|---|---|
| metal ion binding | Binding to a metal ion. |
| UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity | Catalysis of the removal of an acetyl group from the 2-N position of glucosamine in the lipid A precursor UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. |
| UDP-3-O-acyl-N-acetylglucosamine deacetylase activity | Catalysis of the reaction: UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetylglucosamine(2-) + H2O <=> UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine(1-) + acetate. |
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 |
| MMKQRTIATP | VKTVGIGLHS | GRKVTISIKP | APVNSGVQFI | RVDTPERSVV | PATALAVCDT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RLASVIQKDG | VRVSTVEHLL | SACAGLGLDN | LLIELDGEEV | PIMDGSAASF | LFLIESAGIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EQEVPRQFVV | IKKPVEVREG | DKLARLEPFF | GFKLDFTIDF | KHPAVDKTGQ | RFVVDFSEHA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YRSEIGRART | FGFAHEVEAL | REMGLARGGS | LDNAIVLDEH | RILNNEELRY | EDEFVRHKIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DAIGDLYLIG | HPIVGAYVAE | KSGHALNNAL | LRKLLEDPSS | YEISTFAENK | APGAYSQESQ |
| PLFF |