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CAZyme Information: MGYG000001519_01556

You are here: Home > Sequence: MGYG000001519_01556

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 Olsenella sp001457795
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Olsenella; Olsenella sp001457795
CAZyme ID MGYG000001519_01556
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
382 MGYG000001519_13|CGC1 40345.32 4.5606
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001519 1818311 Isolate not provided not provided
Gene Location Start: 817120;  End: 818268  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001519_01556.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE9 7 376 1.6e-122 0.9946380697050938

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 6.38e-151 4 376 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 7.19e-146 4 381 2 380
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 5.17e-89 2 376 3 379
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 4.13e-47 41 379 42 379
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 4.20e-17 49 379 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACV51489.1 6.85e-188 1 380 1 386
ATC60686.1 8.38e-159 1 382 1 382
QIW54244.1 8.38e-159 1 382 1 382
QIW61033.1 1.69e-158 1 382 1 382
QIW58843.1 1.69e-158 1 382 1 382

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 5.89e-62 2 376 3 384
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]
6FV3_A 4.52e-47 20 381 33 394
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]
1O12_A 7.08e-47 52 380 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]
6FV4_A 6.57e-46 20 381 33 394
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 1.64e-42 25 380 38 402
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96166 9.88e-72 41 380 48 386
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3 1.18e-70 31 377 27 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O34450 3.22e-61 2 376 3 384
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 1.40e-60 49 376 53 379
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q6P0U0 6.91e-47 32 382 45 404
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 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
1.000061 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001519_01556.