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CAZyme Information: MGYG000000010_02051

You are here: Home > Sequence: MGYG000000010_02051

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_A lentus
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus_A; Staphylococcus_A lentus
CAZyme ID MGYG000000010_02051
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
384 42115.46 4.9769
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000010 2726400 Isolate United Kingdom Europe
Gene Location Start: 12305;  End: 13459  Strand: +

Full Sequence      Download help

MGHYILDNAV  IYTEQGKIEN  GYIEIQDGYI  QDIQEGSYSG  NLEVVDVNGQ  HIIPGFIDIH60
IHGGYGQDAM  DATPETLNIL  SENLLSEGTT  SFLATTMTQS  SEAINKALKN  VAEYKPLDDK120
RAEILGVHLE  GPFISEHKVG  AQNPKYVARP  SVAKFEAFQS  VAKDKIKIIT  IAPEVEGAKE180
TIQALNDKVI  FSAGHTITDY  DGIEEAVDNG  LQHITHLYNA  QTTFTHREPG  VFGAALTDER240
LTTEVIVDGV  HSHPASVKLA  YLSKGNKNFC  VITDAMRAKG  MKDGEYDLGG  QNVHVKDHEA300
RLENGSLAGS  ILLMNKGLKN  LMNYANIPLE  EAWRTTSLNQ  AIRLNVEDRL  GSIKKGKQAD360
LVIVDSEINV  LTTIKKGYII  DNEQ384

Enzyme Prediction      help

No EC number prediction in MGYG000000010_02051.

CAZyme Signature Domains help

Created with Snap19385776961151341531721922112302492682883073263453647377CE9
Family Start End Evalue family coverage
CE9 7 377 1.6e-135 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap19385776961151341531721922112302492682883073263453644377NagA4380NagA4377nagA4383nagA52380Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 9.36e-175 4 377 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 3.90e-154 4 380 2 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.15e-119 4 377 5 379
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.19e-76 4 383 2 382
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.85e-20 52 380 2 335
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

Created with Snap19385776961151341531721922112302492682883073263453641384QMU11455.1|CE91383QJF25509.1|CE91383QQT14323.1|CE91383QQY20376.1|CE91383ARB40389.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QMU11455.1 3.15e-278 1 384 1 384
QJF25509.1 1.23e-229 1 383 1 383
QQT14323.1 1.74e-229 1 383 1 383
QQY20376.1 1.74e-229 1 383 1 383
ARB40389.1 7.08e-229 1 383 1 383

PDB Hits      download full data without filtering help

Created with Snap193857769611513415317219221123024926828830732634536453792VHL_A303801O12_A43773EGJ_A43776JKU_A43771YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 6.87e-105 5 379 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 3.62e-66 30 380 20 372
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]
3EGJ_A 3.71e-55 4 377 5 376
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]
6JKU_A 2.16e-53 4 377 19 390
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]
1YMY_A 2.21e-53 4 377 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 Snap19385776961151341531721922112302492682883073263453645379sp|O34450|NAGA_BACSU5379sp|Q84F86|NAGA_LYSSH3380sp|P96166|NAGA_VIBFU4370sp|Q8XAC3|AGAA_ECO574377sp|P44537|NAGA_HAEIN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 3.76e-104 5 379 6 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 2.53e-91 5 379 7 381
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166 3.57e-69 3 380 8 385
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3 1.85e-66 4 370 3 365
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P44537 2.65e-55 4 377 3 376
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
1.000044 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000010_02051.