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CAZyme Information: MGYG000001323_01911

You are here: Home > Sequence: MGYG000001323_01911

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 Providencia rettgeri_D
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rettgeri_D
CAZyme ID MGYG000001323_01911
CAZy Family CE11
CAZyme Description UDP-3-O-acyl-N-acetylglucosamine deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
305 MGYG000001323_30|CGC1 33772.72 5.0668
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001323 4749568 Isolate not provided not provided
Gene Location Start: 185873;  End: 186790  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 7.4e-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 1.42e-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

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBV03569.1 1.61e-222 1 305 1 305
QLR02459.1 1.61e-222 1 305 1 305
QLI96711.1 1.61e-222 1 305 1 305
BBU96897.1 1.61e-222 1 305 1 305
QIF65210.1 1.61e-222 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 6.66e-205 1 305 1 305
CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli]
3NZK_A 8.31e-205 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 2.23e-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 3.73e-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 1.17e-128 1 301 2 301
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
B4F105 2.80e-208 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Proteus mirabilis (strain HI4320) OX=529507 GN=lpxC PE=3 SV=1
Q7N153 1.55e-205 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=lpxC PE=3 SV=2
B5R2N0 3.13e-205 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella enteritidis PT4 (strain P125109) OX=550537 GN=lpxC PE=3 SV=1
C0Q5J2 3.13e-205 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella paratyphi C (strain RKS4594) OX=476213 GN=lpxC PE=3 SV=1
B5FI78 3.13e-205 1 305 1 305
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Salmonella dublin (strain CT_02021853) OX=439851 GN=lpxC PE=3 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
1.000030 0.000029 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001323_01911.