Species | Campylobacter sp013416015 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter; Campylobacter sp013416015 | |||||||||||
CAZyme ID | MGYG000000755_00775 | |||||||||||
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: 56514; End: 57404 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 3 | 272 | 3.2e-104 | 0.992619926199262 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK13186 | lpxC | 4.29e-156 | 1 | 296 | 2 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
pfam03331 | LpxC | 1.24e-147 | 3 | 273 | 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. |
COG0774 | LpxC | 1.21e-141 | 1 | 296 | 2 | 300 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
TIGR00325 | lpxC | 3.55e-122 | 1 | 296 | 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] |
PRK13188 | PRK13188 | 4.24e-74 | 1 | 283 | 3 | 310 | 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 |
---|---|---|---|---|---|
QLI04795.1 | 5.49e-205 | 1 | 296 | 1 | 296 |
ARR04465.1 | 2.31e-134 | 1 | 296 | 1 | 294 |
ARR02921.1 | 3.28e-134 | 1 | 296 | 1 | 294 |
QKF56314.1 | 4.83e-134 | 1 | 296 | 1 | 295 |
ANE33141.1 | 4.83e-134 | 1 | 296 | 1 | 295 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3NZK_A | 4.96e-82 | 1 | 295 | 7 | 302 | 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 | 1.65e-81 | 1 | 295 | 2 | 297 | 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 | 5.68e-81 | 1 | 295 | 2 | 297 | 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] |
4MQY_A | 6.64e-81 | 1 | 295 | 2 | 297 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
5U39_A | 1.15e-76 | 1 | 282 | 4 | 287 | Pseudomonasaeruginosa LpxC in complex with CHIR-090 [Pseudomonas aeruginosa PAO1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A0RQZ8 | 4.39e-133 | 1 | 296 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter fetus subsp. fetus (strain 82-40) OX=360106 GN=lpxC PE=3 SV=1 |
A7I3V4 | 1.25e-132 | 1 | 296 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) OX=360107 GN=lpxC PE=3 SV=1 |
A7GZZ5 | 1.59e-128 | 1 | 296 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter curvus (strain 525.92) OX=360105 GN=lpxC PE=3 SV=1 |
Q9PIZ5 | 5.27e-127 | 1 | 296 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=lpxC PE=3 SV=1 |
Q5HX34 | 5.27e-127 | 1 | 296 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter jejuni (strain RM1221) OX=195099 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999647 | 0.000374 | 0.000027 | 0.000001 | 0.000000 | 0.000002 |
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