Species | UBA1777 sp900549485 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA1777; UBA1777 sp900549485 | |||||||||||
CAZyme ID | MGYG000003668_00702 | |||||||||||
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: 32251; End: 33375 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 4 | 370 | 4.2e-118 | 0.9946380697050938 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00854 | NagA | 1.95e-132 | 1 | 370 | 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 | 2.71e-113 | 3 | 373 | 4 | 378 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
TIGR00221 | nagA | 1.08e-84 | 32 | 370 | 41 | 379 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
PRK11170 | nagA | 3.33e-51 | 38 | 371 | 44 | 377 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
pfam01979 | Amidohydro_1 | 4.98e-13 | 45 | 357 | 2 | 308 | 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 |
---|---|---|---|---|---|
QOX64865.1 | 1.07e-130 | 1 | 370 | 1 | 370 |
CAB1244880.1 | 1.53e-113 | 1 | 370 | 1 | 371 |
QNK41739.1 | 1.18e-112 | 1 | 371 | 1 | 372 |
ASM68045.1 | 1.29e-112 | 1 | 366 | 1 | 366 |
CBL22760.1 | 2.31e-110 | 1 | 366 | 1 | 365 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VHL_A | 5.96e-59 | 4 | 356 | 8 | 370 | 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] |
6FV3_A | 9.03e-55 | 39 | 371 | 58 | 390 | 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 | 1.35e-53 | 39 | 371 | 58 | 390 | 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] |
7NUT_A | 3.00e-48 | 30 | 373 | 51 | 401 | 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] |
1YMY_A | 1.52e-42 | 40 | 373 | 46 | 379 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P96166 | 9.91e-62 | 31 | 373 | 43 | 385 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1 |
Q8XAC3 | 1.31e-59 | 47 | 371 | 49 | 373 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
O34450 | 3.26e-58 | 4 | 356 | 8 | 370 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
Q84F86 | 9.74e-54 | 29 | 370 | 38 | 379 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
A7MBC0 | 1.76e-52 | 39 | 373 | 57 | 401 | N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000011 | 0.000034 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
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