A5GKW4
Gene name |
lpxD |
Protein name |
UDP-3-O-acylglucosamine N-acyltransferase |
Names |
|
Species |
Synechococcus sp (strain WH7803) |
KEGG Pathway |
syx:SynWH7803_1153 |
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 A5GKW4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5GKW4-F1 | Predicted | AlphaFoldDB |
No variants for A5GKW4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5GKW4 | |||||
No associated diseases with A5GKW4
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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| carboxysome | An organelle consisting of a proteinaceous coat and enzymes for the fixation of CO(2). It augments the concentration of CO(2) in the vicinity of RuBisCO to increase the efficiency of CO(2) fixation under atmospheric conditions. |
2 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. |
| structural constituent of carboxysome | The action of a molecule that contributes to the structural integrity of a carboxysome, an organelle found in all cyanobacteria and some chemoautotrophs, consisting of a proteinaceous coat and enzymes for the fixation of CO(2). |
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 |
| MRFSQLIAVL | KNGDAGVLST | SEGRDPELRG | AASLERATAD | QLSFLEKGNA | LVGSLESSEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GAVLIPDQQE | LRELAERLQL | AWAVCGDPRL | AFAEALEQLH | PKPSPQAGIH | ASAVIADRVQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LGAGVSIGAR | VCIGDDTRIG | PRTVIHPGVV | IYGNVDIGEG | CELHANAVLH | PGSRIGDRCV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VHSNAVVGSE | GFGFVPTAKG | WRKMPQTGLV | VLEDGVEVGC | GSTIDRPSVG | ETRIGSGTKI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DNLVQIGHGV | VTGRGCALAS | QVGIAGGAQL | GHGVILAGQV | GVANRAVIGD | RAIASSKSGI |
| 310 | 320 | 330 | 340 | 350 | |
| HGEVAAGEVV | SGYPAIPNRL | WLRCSAAFSK | LPEMAKQLRE | LKKQVSSEAT | GGSIEADQ |