Species | UMGS416 sp900542005 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; UMGS416; UMGS416; UMGS416 sp900542005 | |||||||||||
CAZyme ID | MGYG000000922_00772 | |||||||||||
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: 92571; End: 93767 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 5 | 387 | 2.2e-109 | 0.9973190348525469 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00854 | NagA | 1.52e-128 | 4 | 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 | 6.22e-111 | 2 | 392 | 1 | 380 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
TIGR00221 | nagA | 2.18e-83 | 5 | 388 | 7 | 380 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
PRK11170 | nagA | 6.02e-57 | 5 | 388 | 4 | 377 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
COG0044 | AllB | 4.06e-19 | 1 | 398 | 1 | 427 | Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCG54161.1 | 1.23e-148 | 2 | 390 | 3 | 392 |
SCM56970.1 | 1.16e-146 | 2 | 391 | 3 | 393 |
QMU26964.1 | 1.08e-144 | 2 | 391 | 5 | 393 |
ACT95688.1 | 1.83e-143 | 1 | 391 | 1 | 389 |
QNF31515.1 | 2.87e-143 | 2 | 396 | 5 | 398 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6FV3_A | 9.44e-59 | 10 | 390 | 18 | 392 | 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 | 1.42e-57 | 10 | 390 | 18 | 392 | 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] |
2VHL_A | 1.80e-43 | 10 | 395 | 12 | 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] |
7NUT_A | 2.35e-43 | 47 | 391 | 57 | 402 | 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 | 2.67e-42 | 7 | 387 | 6 | 376 | 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 |
---|---|---|---|---|---|---|
Q84F86 | 2.70e-46 | 18 | 388 | 21 | 380 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
Q8JZV7 | 1.66e-45 | 47 | 398 | 57 | 409 | N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1 |
Q5BJY6 | 1.23e-44 | 47 | 395 | 57 | 406 | N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2 |
Q8XAC3 | 6.36e-44 | 9 | 388 | 9 | 373 | N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2 |
Q6P0U0 | 8.13e-44 | 3 | 391 | 13 | 402 | N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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