Q3JEI7
Gene name |
lpxD |
Protein name |
UDP-3-O-acylglucosamine N-acyltransferase |
Names |
|
Species |
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107) |
KEGG Pathway |
noc:Noc_0229 |
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 Q3JEI7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3JEI7-F1 | Predicted | AlphaFoldDB |
No variants for Q3JEI7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3JEI7 | |||||
No associated diseases with Q3JEI7
3 regional properties for Q3JEI7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Hexapeptide repeat | 147 - 181 | IPR001451-1 |
| repeat | Hexapeptide repeat | 225 - 259 | IPR001451-2 |
| domain | UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, non-repeat region | 23 - 87 | IPR020573 |
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 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. |
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 |
| MEIRLSEIAQ | FLGCAIEGDG | EAPIRGIAPL | HQAQASELSF | YTNRKYAAQA | RLSKAGAIIV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GAKDREQFAG | RRLLISDNPY | RDFARVVDRW | FNRSYRPAPG | VHPTAIVGDD | VQIAENCSIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AYCVIEDGVT | IKAHTVLFPF | CYVGAKTILG | EHCLLYPRVT | LLERVRIGHR | VILHPGVVIG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GDGFGFAPDP | PQGYFKVPQV | GWVEIADDVE | VQCNTAIDRG | ALGPTRIGQG | SKIDNLVQVG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HNVEIGEHSI | IVSQVGISGS | SKIGNWVTLA | GQVGLVGHIR | IGDGAVITAQ | SGVAKDVPPK |
| 310 | 320 | 330 | 340 | ||
| AIMTGSPVQP | MMENRRALAE | LNRLRELRKK | VRELERRLTV | LEQVESC |