Species | Succinivibrio sp900552905 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; Succinivibrio; Succinivibrio sp900552905 | |||||||||||
CAZyme ID | MGYG000002582_00658 | |||||||||||
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: 26864; End: 27808 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE11 | 4 | 277 | 2.9e-110 | 0.992619926199262 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK13186 | lpxC | 2.57e-176 | 1 | 296 | 1 | 292 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
COG0774 | LpxC | 7.46e-165 | 1 | 295 | 1 | 294 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
pfam03331 | LpxC | 3.13e-160 | 4 | 278 | 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. |
TIGR00325 | lpxC | 3.35e-136 | 3 | 291 | 2 | 286 | 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 | 1.15e-82 | 1 | 276 | 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 |
---|---|---|---|---|---|
ACQ92159.1 | 2.54e-134 | 1 | 295 | 1 | 295 |
ATG75211.1 | 1.19e-132 | 1 | 300 | 1 | 299 |
ART82894.1 | 1.69e-132 | 1 | 295 | 1 | 295 |
ART80849.1 | 4.83e-132 | 1 | 295 | 1 | 295 |
AEY00637.1 | 2.78e-131 | 1 | 295 | 1 | 295 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3NZK_A | 1.60e-125 | 1 | 289 | 6 | 293 | 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 | 3.51e-123 | 1 | 289 | 1 | 288 | 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 | 1.20e-122 | 1 | 289 | 1 | 288 | 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 | 1.42e-122 | 1 | 289 | 1 | 288 | CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli] |
5N8C_A | 1.65e-101 | 1 | 307 | 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 |
---|---|---|---|---|---|---|
C4LA30 | 5.08e-135 | 1 | 295 | 1 | 295 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Tolumonas auensis (strain DSM 9187 / TA4) OX=595494 GN=lpxC PE=3 SV=1 |
A4SI61 | 1.50e-129 | 1 | 295 | 1 | 295 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Aeromonas salmonicida (strain A449) OX=382245 GN=lpxC PE=3 SV=1 |
A0KPW7 | 1.22e-128 | 1 | 295 | 1 | 295 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) OX=380703 GN=lpxC PE=3 SV=1 |
B0US73 | 7.58e-127 | 1 | 291 | 1 | 290 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Histophilus somni (strain 2336) OX=228400 GN=lpxC PE=3 SV=1 |
Q9CPA5 | 7.58e-127 | 1 | 293 | 1 | 292 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=lpxC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000030 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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