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CAZyme Information: MGYG000004865_00347

You are here: Home > Sequence: MGYG000004865_00347

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
Lineage Bacteria; Spirochaetota; Spirochaetia; Sphaerochaetales; Sphaerochaetaceae; RUG023;
CAZyme ID MGYG000004865_00347
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
387 MGYG000004865_6|CGC1 41945.02 6.3507
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004865 2913052 MAG China Asia
Gene Location Start: 34308;  End: 35471  Strand: -

Full Sequence      Download help

MLFTNARLVL  ENHTVQASLR  TEGPRIKAYG  EHLSALPGEE  VVDCKGLYLA  PGFIDIHSHG60
GGGHDIMDGE  AEDIVLAAKA  HLKHGTTTYY  PTTMTNTDEA  TIHTFECFRE  ARKYGDAIPH120
LEGIHMEGPY  FSPAQAGAQD  PSFIKTPKQE  HYRMFLEKGG  DVIKRISFAP  ELPGAIEMAD180
ALRDTGIVLA  AGHTNATYQE  ISRAFDHGVT  HLTHFYSGMS  TIHREGGFRI  LGTVEAGYLI240
DGLTIELIAD  GMHLPPELLK  MILKLKAHDH  ISLCTDSMRG  ADMPEGPTIL  GPKVGGVKCF300
VEGGIAKMPD  HQAFAGSVAT  TDRLVRVMHQ  KAGLSIAEAV  AMMTINPARV  MHIDGKTGSI360
AVGKQADLVL  FDENIQVSEV  YLSGKRV387

Enzyme Prediction      help

No EC number prediction in MGYG000004865_00347.

CAZyme Signature Domains help

Created with Snap19385877961161351541741932122322512702903093283483673384CE9
Family Start End Evalue family coverage
CE9 3 384 5.3e-110 0.9973190348525469

CDD Domains      download full data without filtering help

Created with Snap19385877961161351541741932122322512702903093283483671384NagA1387NagA37385nagA3387nagA48387Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.77e-119 1 384 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 8.87e-95 1 387 2 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 7.49e-72 37 385 42 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 4.58e-47 3 387 4 379
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 3.87e-24 48 387 1 324
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 Snap19385877961161351541741932122322512702903093283483671387QTQ14483.1|CE91387QTQ16716.1|CE91387QTQ11346.1|CE931385AEV28731.1|CE92387ADY12033.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QTQ14483.1 6.39e-173 1 387 1 407
QTQ16716.1 3.67e-172 1 387 1 407
QTQ11346.1 2.11e-171 1 387 1 407
AEV28731.1 1.95e-151 31 385 35 388
ADY12033.1 5.12e-138 2 387 3 393

PDB Hits      download full data without filtering help

Created with Snap193858779611613515417419321223225127029030932834836713772VHL_A493876FV3_A493876FV4_A493871O12_A333871YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 6.67e-46 1 377 5 377
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 2.82e-45 49 387 64 392
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 4.07e-44 49 387 64 392
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]
1O12_A 9.37e-43 49 387 53 372
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]
1YMY_A 8.14e-40 33 387 34 379
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap19385877961161351541741932122322512702903093283483678385sp|Q84F86|NAGA_LYSSH49385sp|Q8XAC3|AGAA_ECO571377sp|O34450|NAGA_BACSU42387sp|Q6P0U0|NAGA_DANRE33387sp|P0AF19|NAGA_ECO57
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q84F86 2.62e-48 8 385 6 380
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3 2.30e-46 49 385 47 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O34450 3.65e-45 1 377 5 377
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q6P0U0 9.33e-41 42 387 56 401
N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
P0AF19 4.46e-39 33 387 34 379
N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=nagA 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
1.000048 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004865_00347.