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CAZyme Information: MGYG000001253_00668
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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 | Paramuribaculum sp001689535 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp001689535 | |||||||||||
| CAZyme ID | MGYG000001253_00668 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 75163; End: 76329 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 45 | 363 | 5.4e-85 | 0.9444444444444444 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 1.18e-105 | 46 | 381 | 1 | 339 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
| pfam13088 | BNR_2 | 9.36e-28 | 88 | 356 | 14 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 2.57e-13 | 55 | 374 | 271 | 655 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13088 | BNR_2 | 1.06e-09 | 66 | 251 | 118 | 278 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00260 | Sialidase | 2.35e-07 | 53 | 347 | 9 | 323 | sialidases/neuraminidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQR09640.1 | 5.26e-148 | 41 | 386 | 37 | 382 |
| ANU63021.2 | 1.01e-147 | 41 | 386 | 56 | 401 |
| ASB38906.1 | 1.01e-147 | 41 | 386 | 56 | 401 |
| BBL05903.1 | 1.15e-97 | 41 | 383 | 25 | 375 |
| BCI64112.1 | 2.79e-87 | 45 | 387 | 28 | 375 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4FJ6_A | 1.29e-41 | 40 | 361 | 162 | 506 | Crystalstructure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_B Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_C Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_D Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503] |
| 6MNJ_A | 6.34e-40 | 52 | 361 | 193 | 523 | Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes] |
| 1EUR_A | 1.14e-39 | 52 | 362 | 18 | 347 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 1EUT_A | 3.75e-38 | 52 | 362 | 18 | 347 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
| 6MYV_A | 4.31e-38 | 42 | 361 | 164 | 506 | Sialidase26co-crystallized with DANA-Gc [bacterium],6MYV_B Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_C Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_D Sialidase26 co-crystallized with DANA-Gc [bacterium] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q02834 | 1.11e-37 | 8 | 362 | 24 | 389 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
| P31206 | 7.08e-36 | 39 | 361 | 183 | 528 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
| P10481 | 3.56e-24 | 32 | 322 | 6 | 319 | Sialidase OS=Clostridium perfringens OX=1502 GN=nanH PE=1 SV=1 |
| P15698 | 2.62e-20 | 45 | 322 | 38 | 337 | Sialidase OS=Paeniclostridium sordellii OX=1505 PE=1 SV=1 |
| P29767 | 4.63e-20 | 48 | 359 | 384 | 809 | Sialidase OS=Clostridium septicum OX=1504 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 |
|---|---|---|---|---|---|
| 0.000269 | 0.998937 | 0.000220 | 0.000201 | 0.000183 | 0.000162 |