You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000004270_00745
You are here: Home > Sequence: MGYG000004270_00745
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 | Porphyromonas_A sp900554935 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A sp900554935 | |||||||||||
| CAZyme ID | MGYG000004270_00745 | |||||||||||
| CAZy Family | CE11 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 2544; End: 3974 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE11 | 14 | 234 | 1.6e-71 | 0.8081180811808119 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK13188 | PRK13188 | 0.0 | 12 | 472 | 3 | 464 | bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed |
| pfam03331 | LpxC | 3.10e-119 | 14 | 309 | 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. |
| PRK13186 | lpxC | 9.60e-110 | 13 | 310 | 3 | 275 | UDP-3-O-acyl-N-acetylglucosamine deacetylase. |
| COG0774 | LpxC | 3.04e-90 | 13 | 312 | 3 | 280 | UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]. |
| TIGR00325 | lpxC | 4.35e-68 | 13 | 329 | 2 | 292 | 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 |
|---|---|---|---|---|---|
| VEJ03317.1 | 1.07e-241 | 13 | 469 | 7 | 463 |
| AST54919.1 | 1.24e-218 | 12 | 470 | 2 | 460 |
| QJE30768.1 | 1.24e-218 | 12 | 470 | 2 | 460 |
| QUT94149.1 | 1.24e-218 | 12 | 470 | 2 | 460 |
| QCY57342.1 | 1.24e-218 | 12 | 470 | 2 | 460 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5VWM_A | 2.69e-46 | 2 | 310 | 89 | 374 | Crystalstructure of UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (LpxC) from Pseudomonas aeruginosa in complex with CHIR-090 inhibitor [Pseudomonas aeruginosa PAO1] |
| 5U39_A | 1.16e-45 | 9 | 310 | 1 | 279 | Pseudomonasaeruginosa LpxC in complex with CHIR-090 [Pseudomonas aeruginosa PAO1] |
| 6MO4_A | 2.77e-45 | 11 | 310 | 5 | 281 | Co-Crystalstructure of P. aeruginosa LpxC-50067 complex [Pseudomonas aeruginosa PAO1] |
| 6MO5_A | 2.85e-45 | 11 | 310 | 6 | 282 | Co-Crystalstructure of P. aeruginosa LpxC-50228 complex [Pseudomonas aeruginosa PAO1],6MOD_A Co-Crystal structure of P. aeruginosa LpxC-50432 complex [Pseudomonas aeruginosa] |
| 4J3D_A | 4.62e-45 | 13 | 310 | 3 | 277 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q7MXT8 | 7.63e-214 | 12 | 472 | 2 | 462 | Bifunctional enzyme LpxC/FabZ OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=lpxC/fabZ PE=3 SV=1 |
| Q8A015 | 5.05e-207 | 13 | 470 | 3 | 460 | 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 |
| Q8KBX0 | 7.01e-111 | 14 | 468 | 5 | 463 | Bifunctional enzyme LpxC/FabZ OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=lpxC/fabZ PE=3 SV=1 |
| Q1D2K0 | 1.28e-54 | 10 | 310 | 4 | 279 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=lpxC PE=3 SV=1 |
| B1XT16 | 5.57e-53 | 13 | 337 | 3 | 302 | UDP-3-O-acyl-N-acetylglucosamine deacetylase OS=Polynucleobacter necessarius subsp. necessarius (strain STIR1) OX=452638 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 |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |