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CAZyme Information: MGYG000001378_01868
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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 | Bacteroides ovatus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides ovatus | |||||||||||
| CAZyme ID | MGYG000001378_01868 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 394793; End: 395953 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 50 | 371 | 3.6e-93 | 0.935672514619883 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 8.69e-102 | 48 | 381 | 3 | 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 | 9.19e-33 | 71 | 360 | 2 | 278 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13859 | BNR_3 | 1.18e-16 | 61 | 285 | 1 | 211 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00260 | Sialidase | 1.05e-11 | 55 | 357 | 11 | 327 | 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. |
| COG4409 | NanH | 2.93e-09 | 29 | 349 | 243 | 620 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SCV10539.1 | 1.80e-294 | 1 | 386 | 1 | 386 |
| QRQ57765.1 | 1.80e-294 | 1 | 386 | 1 | 386 |
| QGT71225.1 | 1.80e-294 | 1 | 386 | 1 | 386 |
| ALJ46183.1 | 1.80e-294 | 1 | 386 | 1 | 386 |
| QUT80883.1 | 1.04e-293 | 1 | 386 | 1 | 386 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MNJ_A | 2.06e-38 | 52 | 385 | 193 | 537 | Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes] |
| 6MYV_A | 1.49e-37 | 52 | 385 | 174 | 520 | 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] |
| 6MRV_A | 2.01e-37 | 52 | 385 | 195 | 541 | Sialidase26co-crystallized with DANA [bacterium],6MRV_B Sialidase26 co-crystallized with DANA [bacterium],6MRX_A Sialidase26 apo [bacterium],6MRX_B Sialidase26 apo [bacterium],6MRX_C Sialidase26 apo [bacterium],6MRX_D Sialidase26 apo [bacterium] |
| 2BF6_A | 4.99e-37 | 59 | 386 | 23 | 447 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 5.23e-37 | 59 | 386 | 23 | 447 | TheStructure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK6_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_B The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P31206 | 1.56e-38 | 52 | 385 | 196 | 542 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
| O35657 | 1.93e-35 | 7 | 382 | 24 | 405 | Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1 |
| A5PF10 | 5.77e-35 | 40 | 382 | 59 | 412 | Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 SV=1 |
| Q99PW3 | 6.95e-34 | 7 | 382 | 24 | 405 | Sialidase-1 OS=Rattus norvegicus OX=10116 GN=Neu1 PE=1 SV=1 |
| A6BMK7 | 7.66e-34 | 5 | 382 | 29 | 411 | Sialidase-1 OS=Bos taurus OX=9913 GN=NEU1 PE=2 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000000 | 0.000022 | 1.000040 | 0.000000 | 0.000000 | 0.000000 |