Species | Porphyromonas_A sp001808555 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A sp001808555 | |||||||||||
CAZyme ID | MGYG000003251_00701 | |||||||||||
CAZy Family | GH89 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 532; End: 2058 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 1 | 480 | 2.3e-153 | 0.717948717948718 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam05089 | NAGLU | 4.53e-102 | 1 | 227 | 109 | 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. |
pfam12972 | NAGLU_C | 1.59e-73 | 234 | 478 | 1 | 242 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCA49739.1 | 1.66e-173 | 1 | 498 | 200 | 692 |
QUT70725.1 | 7.98e-173 | 1 | 498 | 217 | 709 |
QUT38035.1 | 4.59e-172 | 1 | 474 | 177 | 645 |
ALJ42460.1 | 4.59e-172 | 1 | 474 | 177 | 645 |
BCA49750.1 | 2.25e-171 | 1 | 482 | 228 | 706 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4XWH_A | 6.66e-97 | 1 | 503 | 215 | 713 | Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
2VC9_A | 1.06e-46 | 1 | 455 | 378 | 831 | 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-46 | 1 | 455 | 386 | 839 | 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 | 7.02e-46 | 1 | 455 | 401 | 854 | 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 | 2.92e-97 | 1 | 503 | 238 | 736 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
Q9FNA3 | 2.23e-77 | 1 | 503 | 265 | 806 | 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 |
---|---|---|---|---|---|
1.000028 | 0.000015 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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