| Species | Brachyspira pilosicoli | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira pilosicoli | |||||||||||
| CAZyme ID | MGYG000000470_02052 | |||||||||||
| CAZy Family | CE9 | |||||||||||
| CAZyme Description | Glucosamine-6-phosphate deaminase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 3761; End: 5725 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE9 | 271 | 639 | 1.2e-118 | 0.9973190348525469 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1820 | NagA | 4.49e-138 | 269 | 640 | 2 | 376 | N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]. |
| PRK11170 | nagA | 1.20e-136 | 269 | 645 | 2 | 382 | N-acetylglucosamine-6-phosphate deacetylase; Provisional |
| cd00854 | NagA | 3.88e-128 | 269 | 639 | 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. |
| TIGR00221 | nagA | 2.38e-100 | 269 | 640 | 5 | 380 | N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars] |
| PRK00443 | nagB | 3.43e-47 | 1 | 253 | 1 | 261 | glucosamine-6-phosphate deaminase; Provisional |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGA65840.1 | 0.0 | 1 | 654 | 1 | 654 |
| CCG56996.1 | 0.0 | 1 | 654 | 1 | 654 |
| ADK30104.1 | 0.0 | 1 | 654 | 1 | 654 |
| AFR70723.1 | 0.0 | 1 | 654 | 1 | 654 |
| ASJ22234.1 | 0.0 | 1 | 654 | 1 | 654 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3EGJ_A | 7.71e-106 | 269 | 643 | 5 | 380 | N-acetylglucosamine-6-phosphatedeacetylase 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] |
| 1YMY_A | 1.04e-95 | 269 | 640 | 2 | 377 | 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] |
| 2P53_A | 5.74e-95 | 269 | 640 | 2 | 377 | ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12] |
| 6JKU_A | 2.69e-84 | 256 | 642 | 3 | 393 | 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] |
| 7NUT_A | 9.39e-49 | 310 | 639 | 55 | 398 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O32445 | 3.83e-105 | 269 | 643 | 2 | 377 | 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 |
| P0AF19 | 5.69e-95 | 269 | 640 | 2 | 377 | N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=nagA PE=2 SV=1 |
| P0AF18 | 5.69e-95 | 269 | 640 | 2 | 377 | N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1 |
| P44537 | 3.49e-84 | 269 | 643 | 3 | 380 | N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA PE=3 SV=1 |
| Q6P0U0 | 2.72e-52 | 310 | 639 | 55 | 398 | 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 |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.