Species | Phyllobacterium sp900539805 | |||||||||||
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Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales_A; Rhizobiaceae_A; Phyllobacterium; Phyllobacterium sp900539805 | |||||||||||
CAZyme ID | MGYG000002827_03806 | |||||||||||
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: 21382; End: 22401 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 2 | 297 | 4e-85 | 0.7721179624664879 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00854 | NagA | 3.13e-71 | 2 | 296 | 49 | 335 | 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 | 9.21e-67 | 1 | 296 | 49 | 336 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
TIGR00221 | nagA | 1.23e-45 | 2 | 295 | 54 | 339 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
PRK11170 | nagA | 5.68e-31 | 2 | 308 | 51 | 342 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
pfam01979 | Amidohydro_1 | 2.62e-06 | 1 | 221 | 1 | 204 | 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 |
---|---|---|---|---|---|
QND50578.1 | 4.10e-201 | 1 | 337 | 1 | 337 |
AMJ63215.1 | 2.60e-152 | 2 | 332 | 3 | 333 |
AOO79157.1 | 4.95e-150 | 2 | 331 | 3 | 332 |
BCB17561.1 | 7.16e-147 | 1 | 336 | 1 | 336 |
QCI64079.1 | 3.02e-145 | 1 | 331 | 1 | 331 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6FV3_A | 2.06e-36 | 2 | 277 | 64 | 329 | Crystalstructure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_B Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_C Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155],6FV3_D Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis. [Mycolicibacterium smegmatis MC2 155] |
6FV4_A | 2.86e-35 | 2 | 277 | 64 | 329 | Thestructure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155],6FV4_B The structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155] |
1YMY_A | 1.42e-30 | 1 | 295 | 50 | 336 | CrystalStructure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YMY_B Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YRR_A Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],1YRR_B Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],2P50_A Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_B Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_C Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_D Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12] |
2VHL_A | 4.62e-30 | 1 | 295 | 54 | 344 | 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] |
2P53_A | 7.18e-30 | 1 | 295 | 50 | 336 | ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0AF18 | 7.75e-30 | 1 | 295 | 50 | 336 | N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1 |
P0AF19 | 7.75e-30 | 1 | 295 | 50 | 336 | N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=nagA PE=2 SV=1 |
A7MBC0 | 8.35e-30 | 1 | 335 | 62 | 400 | N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1 |
Q8XAC3 | 1.37e-29 | 1 | 295 | 46 | 332 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
O34450 | 2.53e-29 | 1 | 295 | 54 | 344 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000037 | 0.000012 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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