Species | Providencia rettgeri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rettgeri | |||||||||||
CAZyme ID | MGYG000004295_01991 | |||||||||||
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: 9193; End: 10110 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 4 | 276 | 7.4e-121 | 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 | 1.95e-178 | 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 | 2.01e-90 | 1 | 279 | 2 | 301 | 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 |
---|---|---|---|---|---|
QWQ18080.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
QIF61173.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
AWS52388.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
QZY65632.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
QWQ21914.1 | 6.56e-222 | 1 | 305 | 1 | 305 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4MQY_A | 4.69e-205 | 1 | 305 | 1 | 305 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
3NZK_A | 1.38e-203 | 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] |
4MDT_A | 1.57e-203 | 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 | 7.53e-203 | 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 | 5.80e-129 | 1 | 302 | 2 | 302 | 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 |
---|---|---|---|---|---|---|
B4F105 | 4.64e-207 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Proteus mirabilis (strain HI4320) OX=529507 GN=lpxC PE=3 SV=1 |
P0A725 | 2.57e-204 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=lpxC PE=1 SV=1 |
P0A727 | 2.57e-204 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=lpxC PE=3 SV=1 |
P0A726 | 2.57e-204 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=lpxC PE=3 SV=1 |
B7UIE6 | 2.57e-204 | 1 | 305 | 1 | 305 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) OX=574521 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000030 | 0.000029 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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