You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000147_00440
You are here: Home > Sequence: MGYG000000147_00440
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 | Bacillus paralicheniformis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis | |||||||||||
| CAZyme ID | MGYG000000147_00440 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | Pectate lyase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 429862; End: 431169 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 142 | 351 | 5.7e-98 | 0.9953051643192489 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 3.17e-71 | 24 | 434 | 23 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 7.35e-59 | 152 | 354 | 12 | 189 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 8.54e-44 | 127 | 351 | 8 | 211 | Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| VEB18559.1 | 0.0 | 1 | 435 | 1 | 435 |
| BAL45988.1 | 0.0 | 1 | 435 | 1 | 435 |
| QEO06625.1 | 0.0 | 1 | 435 | 1 | 435 |
| QFY39273.1 | 0.0 | 1 | 435 | 1 | 435 |
| AUZ30128.1 | 0.0 | 1 | 435 | 1 | 435 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1VBL_A | 1.23e-164 | 26 | 434 | 2 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1BN8_A | 2.69e-157 | 8 | 434 | 4 | 419 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 7.66e-157 | 8 | 434 | 4 | 419 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 5AMV_A | 4.27e-156 | 25 | 434 | 1 | 398 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
| 2NZM_A | 3.47e-155 | 25 | 434 | 1 | 398 | ChainA, Pectate lyase [Bacillus subtilis],2O04_A Chain A, Pectate lyase [Bacillus subtilis],2O0V_A Chain A, Pectate lyase [Bacillus subtilis],2O0W_A Chain A, Pectate lyase [Bacillus subtilis],2O17_A Chain A, Pectate lyase [Bacillus subtilis],2O1D_A Chain A, Pectate lyase [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39116 | 1.47e-156 | 8 | 434 | 4 | 419 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| Q59671 | 1.73e-76 | 9 | 434 | 16 | 380 | Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel PE=3 SV=1 |
| Q51915 | 2.44e-76 | 15 | 434 | 20 | 380 | Pectate lyase OS=Pseudomonas marginalis OX=298 GN=pel PE=1 SV=1 |
| Q56806 | 4.90e-75 | 11 | 434 | 16 | 377 | Pectate lyase OS=Xanthomonas campestris pv. malvacearum OX=86040 PE=3 SV=1 |
| Q60140 | 1.17e-73 | 25 | 434 | 29 | 379 | Pectate lyase OS=Pseudomonas viridiflava OX=33069 GN=pel PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000244 | 0.999078 | 0.000166 | 0.000184 | 0.000162 | 0.000146 |