Species | UBA5394 sp900542615 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; UBA5394; UBA5394 sp900542615 | |||||||||||
CAZyme ID | MGYG000000898_01191 | |||||||||||
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: 2974; End: 4104 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 4 | 372 | 2.4e-127 | 0.9946380697050938 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00854 | NagA | 1.98e-132 | 1 | 372 | 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 | 1.46e-118 | 2 | 372 | 8 | 375 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
TIGR00221 | nagA | 3.98e-83 | 2 | 373 | 11 | 380 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
PRK11170 | nagA | 3.63e-44 | 39 | 372 | 42 | 376 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
pfam01979 | Amidohydro_1 | 2.76e-21 | 47 | 360 | 1 | 309 | 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 |
---|---|---|---|---|---|
QIA31363.1 | 3.11e-110 | 1 | 376 | 1 | 372 |
ANU41013.1 | 3.11e-110 | 1 | 376 | 1 | 372 |
QQR06201.1 | 3.11e-110 | 1 | 376 | 1 | 372 |
ADZ84961.1 | 3.05e-109 | 1 | 376 | 1 | 379 |
QEH70419.1 | 3.05e-109 | 1 | 376 | 1 | 379 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VHL_A | 2.65e-57 | 48 | 360 | 55 | 372 | 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 | 4.75e-53 | 19 | 374 | 30 | 400 | 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] |
1O12_A | 6.39e-46 | 50 | 372 | 55 | 369 | 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] |
6FV3_A | 7.89e-46 | 25 | 372 | 41 | 389 | 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 | 1.14e-44 | 25 | 372 | 41 | 389 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q84F86 | 1.64e-64 | 3 | 374 | 8 | 381 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
Q8XAC3 | 6.46e-61 | 50 | 376 | 49 | 376 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
O34450 | 1.45e-56 | 48 | 360 | 55 | 372 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
A7MBC0 | 5.52e-56 | 2 | 374 | 19 | 400 | N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1 |
P96166 | 2.36e-55 | 48 | 374 | 57 | 384 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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