Species | Citrobacter_A sedlakii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sedlakii | |||||||||||
CAZyme ID | MGYG000001700_02941 | |||||||||||
CAZy Family | CE11 | |||||||||||
CAZyme Description | UDP-3-O-acyl-N-acetylglucosamine deacetylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 118205; End: 119122 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 4 | 276 | 5.1e-122 | 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 | 3.37e-179 | 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 | 4.37e-89 | 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 |
---|---|---|---|---|---|
QUC29367.1 | 3.96e-223 | 1 | 305 | 1 | 305 |
AMG93320.1 | 4.62e-222 | 1 | 305 | 1 | 305 |
AUO65819.1 | 4.62e-222 | 1 | 305 | 1 | 305 |
CBG86882.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
QBY31356.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4MDT_A | 3.81e-220 | 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] |
4MQY_A | 2.20e-219 | 1 | 305 | 1 | 305 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
3P3G_A | 5.03e-217 | 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] |
3NZK_A | 4.89e-213 | 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] |
5N8C_A | 2.88e-129 | 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 |
---|---|---|---|---|---|---|
B7LWG2 | 2.65e-222 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73) OX=585054 GN=lpxC PE=3 SV=1 |
A8ALK0 | 6.24e-221 | 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 |
B5R2N0 | 4.21e-219 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella enteritidis PT4 (strain P125109) OX=550537 GN=lpxC PE=3 SV=1 |
B5F7X0 | 4.21e-219 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella agona (strain SL483) OX=454166 GN=lpxC PE=3 SV=1 |
B5FI78 | 4.21e-219 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella dublin (strain CT_02021853) OX=439851 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000028 | 0.000007 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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