Species | Campylobacter_B sp900539505 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter_B; Campylobacter_B sp900539505 | |||||||||||
CAZyme ID | MGYG000003713_01241 | |||||||||||
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: 52676; End: 53560 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 3 | 270 | 2.6e-107 | 0.992619926199262 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK13186 | lpxC | 4.70e-170 | 1 | 286 | 2 | 289 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
pfam03331 | LpxC | 8.13e-157 | 3 | 271 | 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 | 1.08e-153 | 1 | 294 | 2 | 300 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
TIGR00325 | lpxC | 1.17e-132 | 1 | 279 | 1 | 281 | 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 | 1.20e-74 | 1 | 286 | 3 | 320 | 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 |
---|---|---|---|---|---|
AKT92102.1 | 3.45e-207 | 1 | 294 | 1 | 294 |
ABS52292.1 | 3.68e-170 | 1 | 294 | 1 | 294 |
QKF70723.1 | 2.99e-167 | 1 | 294 | 1 | 295 |
QKF86666.1 | 7.78e-163 | 1 | 294 | 1 | 295 |
QPH85895.1 | 1.07e-162 | 1 | 294 | 1 | 294 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3NZK_A | 3.56e-84 | 1 | 279 | 7 | 290 | 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 | 4.76e-83 | 1 | 279 | 2 | 285 | 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 | 5.76e-83 | 1 | 279 | 2 | 285 | 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 | 6.74e-83 | 1 | 279 | 2 | 285 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
5U39_A | 7.95e-82 | 1 | 279 | 4 | 286 | Pseudomonasaeruginosa LpxC in complex with CHIR-090 [Pseudomonas aeruginosa PAO1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A7I3V4 | 7.36e-171 | 1 | 294 | 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 |
A7ZC65 | 6.10e-163 | 1 | 294 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter concisus (strain 13826) OX=360104 GN=lpxC PE=3 SV=1 |
A0RQZ8 | 1.01e-161 | 1 | 294 | 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 |
A7GZZ5 | 5.82e-161 | 1 | 294 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter curvus (strain 525.92) OX=360105 GN=lpxC PE=3 SV=1 |
B9KEU6 | 5.04e-148 | 1 | 294 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) OX=306263 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000045 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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