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CAZyme Information: MGYG000001421_01241

You are here: Home > Sequence: MGYG000001421_01241

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 Dielma fastidiosa
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Dielma; Dielma fastidiosa
CAZyme ID MGYG000001421_01241
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
400 MGYG000001421_3|CGC3 43834.97 4.8182
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001421 3575388 Isolate not provided not provided
Gene Location Start: 180727;  End: 181929  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001421_01241.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE9 5 373 2.9e-88 0.9919571045576407

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 2.14e-97 1 373 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 1.53e-90 1 378 2 380
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 3.30e-57 4 374 8 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 1.51e-41 115 369 126 372
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 6.14e-17 46 361 2 309
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
BBB48842.1 1.49e-132 1 393 1 390
QIA42332.1 2.15e-127 5 392 5 394
ATO99271.1 2.15e-127 5 392 5 394
QIK57080.1 4.69e-127 1 390 1 383
AOT69371.1 1.13e-112 4 391 6 393

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 7.19e-36 1 381 5 392
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]
7NUT_A 2.77e-31 36 380 53 405
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]
1YMY_A 3.29e-30 115 376 126 379
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 1.63e-29 115 376 126 379
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
1O12_A 1.40e-28 12 379 25 375
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96166 2.83e-44 46 379 57 388
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3 2.02e-36 2 375 4 374
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O34450 3.94e-35 1 381 5 392
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0 9.46e-35 36 381 53 406
N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
P44537 5.53e-33 8 374 10 377
N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA PE=3 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 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001421_01241.