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CAZyme Information: MGYG000003388_01694

You are here: Home > Sequence: MGYG000003388_01694

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 Neisseria subflava_C
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Neisseriaceae; Neisseria; Neisseria subflava_C
CAZyme ID MGYG000003388_01694
CAZy Family CE11
CAZyme Description UDP-3-O-acyl-N-acetylglucosamine deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
304 33670.41 4.8784
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003388 2136685 MAG United States North America
Gene Location Start: 407038;  End: 407952  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.5.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE11 3 277 2.5e-111 0.992619926199262

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK13186 lpxC 5.18e-168 1 300 2 295
UDP-3-O-acyl-N-acetylglucosamine deacetylase.
COG0774 LpxC 3.75e-165 1 303 2 300
UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis].
pfam03331 LpxC 2.77e-153 3 278 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 1.62e-116 1 298 1 293
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 5.76e-84 1 276 3 298
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
QXW93928.1 5.82e-220 1 304 1 304
QXW90794.1 5.82e-220 1 304 1 304
QKI22877.1 7.93e-218 1 304 1 304
QCL69616.1 6.51e-217 1 304 1 304
QCL71644.1 3.10e-215 1 304 1 304

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4MDT_A 1.68e-106 3 298 4 297
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 2.01e-106 3 298 4 297
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]
3NZK_A 2.05e-106 3 298 9 302
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]
4MQY_A 2.38e-106 3 298 4 297
CrystalStructure of the Escherichia coli LpxC/LPC-138 complex [Escherichia coli]
5N8C_A 3.05e-104 3 304 5 303
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
Q9JWS2 4.11e-208 1 301 1 301
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=lpxC PE=3 SV=1
Q9K1Q3 5.84e-208 1 301 1 301
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=lpxC PE=3 SV=1
A9LZR8 5.84e-208 1 301 1 301
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Neisseria meningitidis serogroup C (strain 053442) OX=374833 GN=lpxC PE=3 SV=1
Q5F569 8.29e-208 1 301 1 301
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=lpxC PE=3 SV=1
A1KR52 2.38e-207 1 301 1 301
UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) OX=272831 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
1.000038 0.000010 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003388_01694.