Species | Phanerochaete chrysosporium | |||||||||||
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Lineage | Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium | |||||||||||
CAZyme ID | AGR57_4676T0-p1 | |||||||||||
CAZy Family | GH30 | |||||||||||
CAZyme Description | Carbohydrate Esterase Family 9 protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 11 | 282 | 4.2e-63 | 0.6300268096514745 |
CE9 | 363 | 507 | 4.5e-45 | 0.3780160857908847 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
238434 | NagA | 5.13e-108 | 8 | 507 | 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. |
224733 | NagA | 1.14e-86 | 57 | 510 | 38 | 378 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
272968 | nagA | 1.12e-58 | 53 | 508 | 38 | 380 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
183010 | nagA | 3.61e-45 | 61 | 511 | 43 | 380 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
396526 | Amidohydro_1 | 1.21e-13 | 367 | 510 | 179 | 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 |
---|---|---|---|---|---|
1.68e-183 | 1 | 513 | 1 | 497 | |
1.36e-182 | 1 | 513 | 1 | 497 | |
1.80e-180 | 1 | 513 | 1 | 497 | |
6.60e-127 | 262 | 515 | 1 | 245 | |
1.46e-115 | 10 | 514 | 18 | 433 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.62e-76 | 10 | 517 | 15 | 408 | Chain A, 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] |
|
1.01e-34 | 67 | 507 | 53 | 384 | The Three-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] |
|
1.68e-32 | 5 | 508 | 2 | 377 | N-acetylglucosamine-6-phosphate deacetylase 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] |
|
2.31e-29 | 64 | 510 | 46 | 379 | Crystal Structure 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] |
|
1.09e-28 | 64 | 510 | 46 | 379 | Chain A, 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 |
---|---|---|---|---|---|---|
3.05e-81 | 1 | 507 | 20 | 409 | N-acetylglucosamine-6-phosphate deacetylase OS=Drosophila melanogaster OX=7227 GN=CG17065 PE=2 SV=1 |
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2.12e-77 | 3 | 513 | 8 | 404 | N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1 |
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1.89e-76 | 7 | 517 | 12 | 408 | N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1 |
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2.89e-75 | 10 | 517 | 15 | 408 | N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2 |
|
7.35e-75 | 2 | 511 | 15 | 414 | N-acetylglucosamine-6-phosphate deacetylase OS=Caenorhabditis elegans OX=6239 GN=F59B2.3 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000041 | 0.000000 |
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