You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000305_01271
You are here: Home > Sequence: MGYG000000305_01271
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 | RF16 sp900542355 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; RF16; RF16 sp900542355 | |||||||||||
| CAZyme ID | MGYG000000305_01271 | |||||||||||
| CAZy Family | CE11 | |||||||||||
| CAZyme Description | UDP-3-O-acyl-N-acetylglucosamine deacetylase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 68414; End: 69313 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE11 | 3 | 227 | 1.4e-73 | 0.8302583025830258 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK13188 | PRK13188 | 2.58e-150 | 1 | 297 | 3 | 302 | bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed |
| pfam03331 | LpxC | 1.19e-124 | 3 | 293 | 1 | 269 | UDP-3-O-acyl N-acetylglycosamine deacetylase. The enzymes in this family catalyze the second step in the biosynthetic pathway for lipid A. |
| PRK13186 | lpxC | 2.47e-116 | 1 | 293 | 2 | 272 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
| COG0774 | LpxC | 2.38e-97 | 1 | 293 | 2 | 275 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
| TIGR00325 | lpxC | 8.54e-71 | 1 | 293 | 1 | 271 | 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] |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AIF26846.1 | 1.54e-129 | 1 | 293 | 1 | 293 |
| ABR37828.1 | 2.12e-110 | 1 | 297 | 1 | 300 |
| QJR54203.1 | 6.19e-110 | 1 | 297 | 2 | 301 |
| AII66294.1 | 6.19e-110 | 1 | 297 | 2 | 301 |
| QJR60999.1 | 6.19e-110 | 1 | 297 | 2 | 301 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5U39_A | 8.18e-51 | 1 | 293 | 4 | 276 | Pseudomonasaeruginosa LpxC in complex with CHIR-090 [Pseudomonas aeruginosa PAO1] |
| 4J3D_A | 8.63e-51 | 1 | 293 | 2 | 274 | Pseudomonasaeruginosa LpxC in complex with a hydroxamate inhibitor [Pseudomonas aeruginosa PAO1],4J3D_B Pseudomonas aeruginosa LpxC in complex with a hydroxamate inhibitor [Pseudomonas aeruginosa PAO1] |
| 5U3B_A | 9.10e-51 | 1 | 293 | 2 | 274 | Pseudomonasaeruginosa LpxC in complex with NVS-LPXC-01 [Pseudomonas aeruginosa PAO1],5U3B_B Pseudomonas aeruginosa LpxC in complex with NVS-LPXC-01 [Pseudomonas aeruginosa PAO1],6MAE_A CHAIN A. UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase PA-LPXC Complexed with (R)-3-((S)-3-(4-(cyclopropylethynyl)phenyl)-2-oxooxazolidin-5-yl)-N-hydroxy-2-methyl-2-(methylsulfonyl)propenamide [Pseudomonas aeruginosa PAO1] |
| 7K99_A | 1.01e-50 | 1 | 293 | 2 | 274 | CrystalStructure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor 19 [Pseudomonas aeruginosa PAO1],7K99_C Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor 19 [Pseudomonas aeruginosa PAO1],7K9A_A Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor [Pseudomonas aeruginosa PAO1],7K9A_C Crystal Structure of P. aeruginosa LpxC with N-Hydroxyformamide inhibitor [Pseudomonas aeruginosa PAO1] |
| 6MO4_A | 1.01e-50 | 1 | 293 | 6 | 278 | Co-Crystalstructure of P. aeruginosa LpxC-50067 complex [Pseudomonas aeruginosa PAO1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8A015 | 4.00e-109 | 1 | 297 | 2 | 301 | Bifunctional enzyme LpxC/FabZ OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=lpxC/fabZ PE=3 SV=1 |
| Q7MXT8 | 8.11e-101 | 2 | 297 | 3 | 301 | Bifunctional enzyme LpxC/FabZ OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=lpxC/fabZ PE=3 SV=1 |
| Q8KBX0 | 1.03e-72 | 3 | 294 | 5 | 302 | Bifunctional enzyme LpxC/FabZ OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=lpxC/fabZ PE=3 SV=1 |
| B1XT16 | 2.19e-56 | 1 | 293 | 2 | 274 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Polynucleobacter necessarius subsp. necessarius (strain STIR1) OX=452638 GN=lpxC PE=3 SV=1 |
| A4SV81 | 6.85e-55 | 1 | 293 | 2 | 274 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) OX=312153 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 |
|---|---|---|---|---|---|
| 1.000044 | 0.000007 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |