| Species | Oceanobacillus jeddahense | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Oceanobacillus; Oceanobacillus jeddahense | |||||||||||
| CAZyme ID | MGYG000001472_00790 | |||||||||||
| 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: 885743; End: 886930 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE9 | 14 | 387 | 1.1e-131 | 0.9839142091152815 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00854 | NagA | 1.87e-172 | 6 | 387 | 1 | 374 | 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. |
| COG1820 | NagA | 1.43e-148 | 15 | 392 | 10 | 380 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
| TIGR00221 | nagA | 2.02e-119 | 4 | 387 | 3 | 379 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
| PRK11170 | nagA | 5.42e-69 | 15 | 393 | 10 | 382 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
| pfam01979 | Amidohydro_1 | 4.36e-25 | 60 | 390 | 2 | 335 | Amidohydrolase family. This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyzes adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBG19209.1 | 8.74e-181 | 1 | 393 | 1 | 391 |
| BAC14863.1 | 8.74e-181 | 1 | 393 | 1 | 391 |
| QHS23332.1 | 5.05e-154 | 1 | 392 | 3 | 391 |
| ALX50704.1 | 6.06e-152 | 58 | 393 | 56 | 389 |
| QKY69954.1 | 3.14e-150 | 15 | 395 | 13 | 388 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2VHL_A | 1.06e-109 | 4 | 395 | 3 | 392 | 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] |
| 1O12_A | 2.35e-63 | 60 | 394 | 53 | 376 | Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution [Thermotoga maritima],1O12_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution [Thermotoga maritima] |
| 7NUT_A | 1.82e-55 | 60 | 392 | 63 | 403 | 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] |
| 3EGJ_A | 1.19e-51 | 15 | 388 | 13 | 377 | N-acetylglucosamine-6-phosphatedeacetylase from Vibrio cholerae. [Vibrio cholerae],3EGJ_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae. [Vibrio cholerae],3IV8_A N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_C N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_D N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae] |
| 6JKU_A | 6.36e-51 | 15 | 388 | 27 | 391 | Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_C Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_D Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O34450 | 5.79e-109 | 4 | 395 | 3 | 392 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
| Q84F86 | 5.81e-84 | 22 | 392 | 21 | 384 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
| P96166 | 4.97e-69 | 60 | 391 | 57 | 386 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1 |
| Q8XAC3 | 5.17e-62 | 60 | 389 | 47 | 374 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
| Q8JZV7 | 2.41e-56 | 60 | 395 | 63 | 406 | 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 |
|---|---|---|---|---|---|
| 1.000065 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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