Species | ||||||||||||
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Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; | |||||||||||
CAZyme ID | MGYG000004772_00912 | |||||||||||
CAZy Family | CE9 | |||||||||||
CAZyme Description | N-acetylglucosamine-6-phosphate deacetylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2638; End: 3183 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 18 | 180 | 3.9e-39 | 0.4316353887399464 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1820 | NagA | 1.92e-47 | 3 | 169 | 1 | 165 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
cd00854 | NagA | 3.70e-46 | 4 | 169 | 1 | 164 | N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling. |
COG0402 | SsnA | 2.84e-08 | 1 | 60 | 1 | 65 | Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]. |
PRK11170 | nagA | 4.69e-07 | 23 | 157 | 21 | 157 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
PRK09228 | PRK09228 | 2.82e-06 | 21 | 60 | 32 | 78 | guanine deaminase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QIA33930.1 | 6.11e-128 | 1 | 181 | 1 | 181 |
AZH70255.1 | 7.07e-127 | 1 | 181 | 1 | 181 |
ATP54175.1 | 1.16e-125 | 1 | 181 | 1 | 181 |
ATP54184.1 | 2.40e-120 | 1 | 181 | 1 | 181 |
BBH50707.1 | 9.40e-86 | 1 | 178 | 1 | 179 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VHL_A | 4.25e-22 | 21 | 167 | 22 | 172 | TheThree-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis],2VHL_B The Three-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis [Bacillus subtilis] |
7NUT_A | 3.81e-08 | 20 | 148 | 35 | 160 | ChainA, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUT_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_A Chain A, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O34450 | 2.33e-21 | 21 | 167 | 22 | 172 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
Q8XAC3 | 4.12e-17 | 3 | 145 | 2 | 139 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
Q84F86 | 7.43e-16 | 46 | 173 | 50 | 174 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
P96166 | 1.14e-13 | 50 | 179 | 57 | 183 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1 |
Q8JZV7 | 1.83e-08 | 20 | 148 | 35 | 160 | N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000053 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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