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CAZyme Information: MGYG000002584_02300
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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 | Akkermansia sp900545155 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia sp900545155 | |||||||||||
| CAZyme ID | MGYG000002584_02300 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 19216; End: 20397 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 42 | 376 | 6.4e-96 | 0.97953216374269 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 7.49e-117 | 45 | 376 | 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 | 6.58e-34 | 67 | 357 | 1 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 1.97e-10 | 45 | 335 | 263 | 610 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| cd00260 | Sialidase | 9.30e-10 | 45 | 204 | 3 | 157 | 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. |
| pfam13859 | BNR_3 | 4.22e-07 | 67 | 227 | 9 | 164 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SEH72311.1 | 1.08e-167 | 44 | 382 | 36 | 372 |
| AYQ36531.1 | 1.70e-102 | 45 | 379 | 29 | 369 |
| QDT42616.1 | 1.06e-99 | 5 | 382 | 2 | 383 |
| CAZ95099.1 | 3.09e-99 | 10 | 381 | 8 | 383 |
| QJB31557.1 | 2.72e-98 | 26 | 373 | 20 | 381 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MNJ_A | 3.36e-50 | 48 | 361 | 192 | 522 | Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes] |
| 6MYV_A | 4.47e-48 | 48 | 380 | 173 | 517 | 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 | 6.88e-48 | 48 | 380 | 194 | 538 | 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] |
| 1EUR_A | 2.89e-45 | 48 | 376 | 17 | 355 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 1W8N_A | 8.47e-44 | 48 | 376 | 13 | 351 | Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q02834 | 1.42e-42 | 48 | 376 | 59 | 397 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
| P31206 | 3.00e-42 | 48 | 361 | 195 | 527 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
| O35657 | 8.39e-36 | 51 | 371 | 66 | 399 | Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1 |
| A6BMK7 | 2.47e-35 | 51 | 371 | 72 | 405 | Sialidase-1 OS=Bos taurus OX=9913 GN=NEU1 PE=2 SV=2 |
| A5PF10 | 6.67e-35 | 51 | 376 | 73 | 411 | Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 SV=1 |
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 |
|---|---|---|---|---|---|
| 0.001347 | 0.494785 | 0.503080 | 0.000274 | 0.000272 | 0.000232 |