Species | Prevotella bergensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella bergensis | |||||||||||
CAZyme ID | MGYG000003765_01110 | |||||||||||
CAZy Family | GH89 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 45; End: 1277 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 7 | 396 | 7.4e-107 | 0.5203619909502263 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam12972 | NAGLU_C | 9.11e-106 | 105 | 393 | 1 | 258 | Alpha-N-acetylglucosaminidase (NAGLU) C-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 C-terminal domain has an all alpha helical fold. |
pfam05089 | NAGLU | 1.62e-26 | 7 | 88 | 257 | 333 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AGB28890.1 | 6.94e-216 | 1 | 399 | 377 | 774 |
BCS86259.1 | 4.09e-189 | 1 | 399 | 453 | 838 |
QVJ80311.1 | 5.82e-185 | 1 | 410 | 356 | 754 |
ADE81419.1 | 2.34e-184 | 1 | 410 | 356 | 754 |
QUT88634.1 | 7.24e-164 | 1 | 395 | 359 | 712 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VC9_A | 1.04e-54 | 19 | 400 | 533 | 878 | 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 | 1.09e-54 | 19 | 400 | 541 | 886 | 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 | 3.02e-54 | 19 | 400 | 556 | 901 | CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens] |
4XWH_A | 1.06e-38 | 4 | 395 | 364 | 707 | Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9FNA3 | 3.14e-42 | 4 | 329 | 417 | 755 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
P54802 | 6.40e-38 | 4 | 395 | 387 | 730 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000054 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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