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CAZyme Information: MGYG000000303_00384

You are here: Home > Sequence: MGYG000000303_00384

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Varibaculum cambriense_A
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum cambriense_A
CAZyme ID MGYG000000303_00384
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
393 MGYG000000303_3|CGC3 41988.84 4.8085
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000303 2213433 MAG Sweden Europe
Gene Location Start: 93324;  End: 94505  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000303_00384.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE9 35 383 2.3e-88 0.8927613941018767

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 2.12e-95 4 377 3 368
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 2.32e-93 4 387 5 379
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.54e-56 4 376 8 372
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 7.79e-36 27 387 34 380
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 2.14e-07 41 373 1 311
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIE82888.1 5.89e-130 6 389 5 467
AZQ99971.1 3.72e-122 1 383 1 385
AHU90253.1 3.72e-122 1 383 1 385
AWA44324.1 5.27e-122 1 383 1 385
AWG15911.1 1.50e-121 1 383 1 385

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FV3_A 9.17e-62 42 384 64 390
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 1.39e-60 42 384 64 390
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]
7NUT_A 1.35e-32 19 389 36 404
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]
2VHL_A 4.01e-32 41 325 54 329
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]
3EGJ_A 5.46e-30 7 384 11 377
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q6P0U0 1.02e-33 36 386 57 401
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
Q8XAC3 2.29e-32 41 384 46 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q9Y303 7.41e-32 19 389 36 404
N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
P96166 1.21e-31 23 389 42 388
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O34450 2.20e-31 41 325 54 329
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000045 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000303_00384.