Species | Hafnia alvei | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia alvei | |||||||||||
CAZyme ID | MGYG000002508_03262 | |||||||||||
CAZy Family | CE11 | |||||||||||
CAZyme Description | UDP-3-O-acyl-N-acetylglucosamine deacetylase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 3547728; End: 3548645 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 4 | 276 | 1.8e-120 | 0.992619926199262 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0774 | LpxC | 0.0 | 1 | 302 | 1 | 300 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
PRK13186 | lpxC | 0.0 | 1 | 299 | 1 | 295 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
TIGR00325 | lpxC | 0.0 | 2 | 301 | 1 | 297 | UDP-3-0-acyl N-acetylglucosamine deacetylase. UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase from E. coli , LpxC, was previously designated EnvA. This enzyme is involved in lipid-A precursor biosynthesis. It is essential for cell viability. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] |
pfam03331 | LpxC | 2.15e-177 | 4 | 277 | 1 | 271 | UDP-3-O-acyl N-acetylglycosamine deacetylase. The enzymes in this family catalyze the second step in the biosynthetic pathway for lipid A. |
PRK13188 | PRK13188 | 1.45e-86 | 1 | 275 | 2 | 298 | bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMO80859.1 | 3.25e-222 | 1 | 305 | 1 | 305 |
ANC40818.1 | 3.25e-222 | 1 | 305 | 1 | 305 |
QIP57256.1 | 3.25e-222 | 1 | 305 | 1 | 305 |
AIU74128.1 | 3.25e-222 | 1 | 305 | 1 | 305 |
AWV46038.1 | 3.25e-222 | 1 | 305 | 1 | 305 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3NZK_A | 5.71e-212 | 1 | 305 | 6 | 310 | Structureof LpxC from Yersinia enterocolitica Complexed with CHIR090 Inhibitor [Yersinia enterocolitica],3NZK_B Structure of LpxC from Yersinia enterocolitica Complexed with CHIR090 Inhibitor [Yersinia enterocolitica] |
4MQY_A | 1.78e-209 | 1 | 305 | 1 | 305 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
4MDT_A | 5.96e-208 | 1 | 305 | 1 | 305 | Structureof LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_B Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_C Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli],4MDT_D Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine [Escherichia coli] |
3P3G_A | 1.42e-207 | 1 | 300 | 1 | 300 | CrystalStructure of the Escherichia coli LpxC/LPC-009 complex [Escherichia coli IHE3034],3PS1_A Crystal structure of the Escherichia Coli LPXC/LPC-011 complex [Escherichia coli IHE3034],3PS2_A Crystal structure of the Escherichia Coli LPXC/LPC-012 complex [Escherichia coli IHE3034],3PS3_A Crystal structure of the Escherichia Coli LPXC/LPC-053 complex [Escherichia coli IHE3034],4IS9_A Crystal Structure of the Escherichia coli LpxC/L-161,240 complex [Escherichia coli IHE3034],4IS9_B Crystal Structure of the Escherichia coli LpxC/L-161,240 complex [Escherichia coli IHE3034],4ISA_A Crystal Structure of the Escherichia coli LpxC/BB-78485 complex [Escherichia coli IHE3034] |
5N8C_A | 6.71e-128 | 1 | 304 | 2 | 304 | Crystalstructure of Pseudomonas aeruginosa LpxC complexed with inhibitor [Pseudomonas aeruginosa],5N8C_B Crystal structure of Pseudomonas aeruginosa LpxC complexed with inhibitor [Pseudomonas aeruginosa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A4W6J9 | 2.92e-210 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Enterobacter sp. (strain 638) OX=399742 GN=lpxC PE=3 SV=1 |
A8ALK0 | 2.92e-210 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) OX=290338 GN=lpxC PE=3 SV=1 |
Q8ZIE3 | 4.30e-210 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Yersinia pestis OX=632 GN=lpxC PE=3 SV=2 |
Q66EJ9 | 4.30e-210 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Yersinia pseudotuberculosis serotype I (strain IP32953) OX=273123 GN=lpxC PE=3 SV=2 |
A7FM60 | 4.30e-210 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) OX=349747 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000043 | 0.000005 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.