A4SV81
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 asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus) |
KEGG Pathway |
pnu:Pnuc_0174 |
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 A4SV81
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4SV81-F1 | Predicted | AlphaFoldDB |
No variants for A4SV81
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4SV81 | |||||
No associated diseases with A4SV81
No regional properties for A4SV81
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A4SV81 | |||
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 |
| MMKQRTIAAP | VKTVGIGLHS | GRKVTIVIKP | APINSGVQFV | RIDTPEQSVV | PATALAVCDT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RLASVIQKDG | VRVSTVEHLL | SACAGLGLDN | LLIELDGEEV | PIMDGSAASF | LFLIESAGIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EQEAPRQFVV | IKKAVEVREG | DKLARLEPFF | GFKLDFTIDF | KHPAVDKTGQ | RFIVDFAEHA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YRSEIGRART | FGFAHEVEAL | REMGLARGGS | LDNAIVLDEH | RILNNEELRY | EDEFVRHKIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DAIGDLYLIG | HPIVGAYIAE | KSGHALNNAL | LRKLLDDPST | YEISSFAENK | APAAYSQENQ |
| PLFF |