Species | Bifidobacterium bifidum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium bifidum | |||||||||||
CAZyme ID | MGYG000002396_00211 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 280058; End: 285445 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 323 | 658 | 2.9e-89 | 0.9181286549707602 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 6.63e-86 | 324 | 644 | 9 | 315 | 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. |
COG4409 | NanH | 2.02e-35 | 289 | 639 | 235 | 622 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
cd01834 | SGNH_hydrolase_like_2 | 3.23e-20 | 951 | 1139 | 2 | 186 | SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
cd00229 | SGNH_hydrolase | 3.19e-18 | 953 | 1139 | 1 | 182 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
pfam13472 | Lipase_GDSL_2 | 9.83e-18 | 957 | 1134 | 3 | 174 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QRI58688.1 | 0.0 | 1 | 1795 | 1 | 1795 |
AXM90913.1 | 0.0 | 1 | 1795 | 1 | 1795 |
VEG16937.1 | 0.0 | 1 | 1795 | 1 | 1795 |
BAQ98986.1 | 0.0 | 1 | 1795 | 1 | 1795 |
BBA47921.1 | 0.0 | 1 | 1795 | 1 | 1795 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1EUR_A | 6.72e-105 | 312 | 674 | 5 | 364 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
1EUT_A | 1.13e-104 | 312 | 748 | 5 | 436 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
1WCQ_A | 3.48e-104 | 312 | 748 | 1 | 432 | Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens] |
2BZD_A | 6.46e-104 | 312 | 748 | 1 | 432 | Galactoserecognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_B Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_C Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens] |
1W8N_A | 8.80e-104 | 312 | 748 | 1 | 432 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q02834 | 8.96e-105 | 292 | 748 | 28 | 478 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
P31206 | 2.73e-26 | 329 | 657 | 203 | 528 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
P29767 | 2.47e-23 | 313 | 669 | 380 | 826 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
Q99PW3 | 1.18e-22 | 313 | 648 | 55 | 376 | Sialidase-1 OS=Rattus norvegicus OX=10116 GN=Neu1 PE=1 SV=1 |
A5PF10 | 1.74e-22 | 313 | 648 | 62 | 383 | Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000407 | 0.998781 | 0.000213 | 0.000225 | 0.000191 | 0.000158 |
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