| Species | Paramuribaculum sp009775605 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp009775605 | |||||||||||
| CAZyme ID | MGYG000004636_00449 | |||||||||||
| CAZy Family | GH89 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 5180; End: 6364 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH89 | 63 | 393 | 1.3e-118 | 0.5188536953242836 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam05089 | NAGLU | 1.22e-136 | 121 | 393 | 1 | 287 | Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold. |
| pfam12971 | NAGLU_N | 7.25e-37 | 26 | 106 | 1 | 81 | Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUT48266.1 | 6.17e-208 | 25 | 393 | 23 | 390 |
| QQT79630.1 | 2.65e-204 | 25 | 393 | 23 | 391 |
| QUU09704.1 | 2.65e-204 | 25 | 393 | 23 | 391 |
| ASM67128.1 | 2.65e-204 | 25 | 393 | 23 | 391 |
| QRP58487.1 | 2.65e-204 | 25 | 393 | 23 | 391 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4XWH_A | 3.97e-72 | 27 | 393 | 8 | 397 | Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
| 2VC9_A | 3.65e-59 | 17 | 389 | 163 | 547 | Family89 Glycoside Hydrolase from Clostridium perfringens in complex with 2-acetamido-1,2-dideoxynojirmycin [Clostridium perfringens],2VCA_A Family 89 glycoside hydrolase from Clostridium perfringens in complex with beta-N-acetyl-D-glucosamine [Clostridium perfringens],2VCB_A Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with PUGNAc [Clostridium perfringens],2VCC_A Family 89 Glycoside Hydrolase from Clostridium perfringens [Clostridium perfringens] |
| 7MFK_A | 3.86e-59 | 17 | 389 | 171 | 555 | ChainA, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124] |
| 4A4A_A | 1.11e-58 | 17 | 389 | 186 | 570 | CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P54802 | 4.46e-71 | 27 | 393 | 31 | 420 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
| Q9FNA3 | 3.15e-70 | 17 | 393 | 36 | 450 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000407 | 0.998875 | 0.000179 | 0.000189 | 0.000170 | 0.000157 |
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