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CAZyme Information: MGYG000000235_01419

You are here: Home > Sequence: MGYG000000235_01419

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Enterobacter kobei
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter kobei
CAZyme ID MGYG000000235_01419
CAZy Family CE11
CAZyme Description UDP-3-O-acyl-N-acetylglucosamine deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
305 MGYG000000235_4|CGC4 33989 5.2253
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000235 4917845 Isolate China Asia
Gene Location Start: 211528;  End: 212445  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.5.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE11 4 276 2.3e-121 0.992619926199262

CDD Domains      download full data without filtering help

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 4.15e-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 4.36e-88 1 275 2 298
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QEO02871.1 4.81e-224 1 305 1 305
QFH88887.1 4.81e-224 1 305 1 305
BBV80182.1 4.81e-224 1 305 1 305
QMT05676.1 4.81e-224 1 305 1 305
AYL04969.1 4.81e-224 1 305 1 305

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4MQY_A 3.81e-220 1 305 1 305
CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli]
4MDT_A 1.27e-218 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 8.70e-218 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 2.83e-212 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 5.01e-130 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A4W6J9 3.76e-222 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Enterobacter sp. (strain 638) OX=399742 GN=lpxC PE=3 SV=1
A8ALK0 1.26e-220 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
B7LWG2 1.03e-219 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
B7UIE6 2.09e-219 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
P0A725 2.09e-219 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=lpxC PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000235_01419.