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CAZyme Information: MGYG000000011_00123

You are here: Home > Sequence: MGYG000000011_00123

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 Staphylococcus xylosus_B
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus xylosus_B
CAZyme ID MGYG000000011_00123
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000000011_1|CGC3 41711.77 5.0271
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000011 2927352 Isolate United Kingdom Europe
Gene Location Start: 121154;  End: 122314  Strand: +

Full Sequence      Download help

MNKYVIANGR  IYTENETIEQ  GHILIEDGKI  VQIAEGEYQG  GLTTIDVKGQ  HVLPGFIDIH60
MHGGYGEDAM  DASFEGLKHL  SESLLSEGTT  SFLATTMTQS  DENIIKALKN  IVNYQEHQDS120
LNAASIVGIH  LEGPFISEYK  VGAQNPAYVQ  RPSVEKVQQF  QEIANNQIKV  MTFAPEVEGA180
DETLSTLHDQ  INFSIGHTVA  TFDEVNEAVA  HGAKHVTHLY  NAGTAFEHRN  PGLSGAAWVN240
DGLSTESIVD  GIHSHPASVK  VAYKQKGNKR  FFLITDAMRA  KGMPDGEYDL  GGQNVVVKGS300
EARLASGALA  GSILKMNEGL  KNLIEFTGAS  LDDLWRVTSL  NQAIALKIEG  DKGSIAVGKD360
ADIVVVDNDI  QVLTTIKSGK  VHNFNS386

Enzyme Prediction      help

No EC number prediction in MGYG000000011_00123.

CAZyme Signature Domains help

Created with Snap19385777961151351541731932122312502702893083283473666379CE9
Family Start End Evalue family coverage
CE9 6 379 2.1e-131 0.9973190348525469

CDD Domains      download full data without filtering help

Created with Snap19385777961151351541731932122312502702893083283473664379NagA3384NagA2380nagA3380nagA52381Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 6.87e-171 4 379 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 6.53e-157 3 384 1 380
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.76e-123 2 380 3 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 6.15e-68 3 380 1 377
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 2.12e-20 52 381 2 334
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

Created with Snap19385777961151351541731932122312502702893083283473661386ARD73808.1|CE91386CEF19527.1|CE91386QDW89841.1|CE91386AID00771.1|CE91386AID43426.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
ARD73808.1 3.33e-265 1 386 1 386
CEF19527.1 6.71e-265 1 386 1 386
QDW89841.1 6.71e-265 1 386 1 386
AID00771.1 1.92e-264 1 386 1 386
AID43426.1 2.73e-264 1 386 1 386

PDB Hits      download full data without filtering help

Created with Snap193857779611513515417319321223125027028930832834736653812VHL_A213811O12_A23807NUT_A43803EGJ_A43791YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 7.36e-105 5 381 6 386
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]
1O12_A 5.41e-66 21 381 30 371
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]
7NUT_A 1.07e-48 2 380 17 399
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]
3EGJ_A 3.05e-48 4 380 5 377
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]
1YMY_A 4.58e-47 4 379 2 376
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap19385777961151351541731932122312502702893083283473665381sp|O34450|NAGA_BACSU5381sp|Q84F86|NAGA_LYSSH26380sp|P96166|NAGA_VIBFU4384sp|Q8XAC3|AGAA_ECO571380sp|P34480|NAGA_CAEEL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 4.03e-104 5 381 6 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 9.55e-92 5 381 7 381
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166 6.54e-63 26 380 31 383
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3 2.83e-58 4 384 3 377
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P34480 9.09e-50 1 380 24 411
N-acetylglucosamine-6-phosphate deacetylase OS=Caenorhabditis elegans OX=6239 GN=F59B2.3 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000011_00123.