Species | UMGS1820 sp900769795 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1820; UMGS1820 sp900769795 | |||||||||||
CAZyme ID | MGYG000003560_00911 | |||||||||||
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: 6358; End: 7524 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE9 | 9 | 384 | 2.6e-103 | 0.9839142091152815 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00854 | NagA | 8.99e-123 | 3 | 384 | 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 | 4.46e-102 | 1 | 388 | 1 | 379 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
TIGR00221 | nagA | 2.14e-66 | 8 | 385 | 11 | 380 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
PRK11170 | nagA | 2.64e-46 | 9 | 386 | 9 | 378 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
pfam01979 | Amidohydro_1 | 3.49e-17 | 48 | 387 | 1 | 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 |
---|---|---|---|---|---|
QRX64347.1 | 9.06e-116 | 13 | 388 | 16 | 394 |
QEC65805.1 | 2.84e-114 | 4 | 388 | 7 | 393 |
SCM59668.1 | 7.67e-112 | 13 | 388 | 16 | 394 |
QEC79978.1 | 7.93e-111 | 4 | 388 | 6 | 391 |
SCD19170.1 | 1.24e-110 | 39 | 388 | 46 | 394 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6FV3_A | 4.58e-50 | 7 | 385 | 22 | 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 | 6.73e-49 | 7 | 385 | 22 | 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] |
1O12_A | 1.87e-42 | 51 | 388 | 55 | 373 | 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] |
2VHL_A | 2.11e-36 | 8 | 384 | 11 | 384 | 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] |
6JKU_A | 3.93e-35 | 8 | 385 | 25 | 391 | Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_C Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_D Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q84F86 | 1.08e-46 | 20 | 385 | 24 | 380 | N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1 |
P96166 | 1.71e-38 | 51 | 388 | 59 | 386 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1 |
O34450 | 1.16e-35 | 8 | 384 | 11 | 384 | N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1 |
O32445 | 3.00e-33 | 9 | 385 | 9 | 374 | N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nagA PE=1 SV=2 |
A0KYQ5 | 3.84e-32 | 49 | 388 | 60 | 386 | N-acetylgalactosamine-6-phosphate deacetylase OS=Shewanella sp. (strain ANA-3) OX=94122 GN=agaAII PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000079 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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