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CAZyme Information: MGYG000000391_00114

You are here: Home > Sequence: MGYG000000391_00114

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 UBA11475 sp003538975
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA11475; UBA11475 sp003538975
CAZyme ID MGYG000000391_00114
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000000391_1|CGC1 41415.43 6.3974
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000391 1644097 MAG Sweden Europe
Gene Location Start: 118697;  End: 119857  Strand: +

Full Sequence      Download help

MKGFTNSLVY  LNGGFYKKAV  GIENGRIAYI  GDDYSAITES  LDKADCKSYL  VPGFIDEHIH60
GAGGSDAMDG  TEKALKTISD  TLVKEGTTSF  LFTTMTASPE  KTKASLAAAD  GFIGKYNKQE120
ENGTVTGARP  LGVHLEGPFV  NPVKCGAQPE  EFILEPKICY  LKDFFVKDRL  VKMITVAPEL180
ADDGFIQYLK  DKGITVSAGH  TNATFEEFSA  SVKEGVSCTT  HTYNAMRAFT  HRETGVIGGA240
FLTDVYNELI  ADGIHVSYPA  IRILFGMKSD  KVILITDAMR  AKGLSDGESE  LGGQKVFVKN300
GEARLSDGTL  AGSVLKMNVA  IKNLVLKAGV  PLETVIKSAT  ENPAKNLKIF  ENTGSIEIGK360
NADLTLLSKN  FDVLSVMIGG  KTVYKA386

Enzyme Prediction      help

No EC number prediction in MGYG000000391_00114.

CAZyme Signature Domains help

Created with Snap19385777961151351541731932122312502702893083283473665380CE9
Family Start End Evalue family coverage
CE9 5 380 1.3e-120 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap19385777961151351541731932122312502702893083283473664380NagA1384NagA19381nagA1383nagA49383Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.09e-155 4 380 3 374
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 1.41e-134 1 384 1 379
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.08e-100 19 381 23 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.00e-83 1 383 1 379
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 2.91e-25 49 383 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

Created with Snap19385777961151351541731932122312502702893083283473661385QVK17341.1|CE91385QNU06784.1|CE97386AMN36672.1|CE91385AXN39215.1|CE97386SQI05496.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QVK17341.1 2.15e-102 1 385 2 380
QNU06784.1 4.84e-95 1 385 1 388
AMN36672.1 6.27e-95 7 386 7 378
AXN39215.1 1.37e-94 1 385 1 388
SQI05496.1 5.02e-94 7 386 7 378

PDB Hits      download full data without filtering help

Created with Snap1938577796115135154173193212231250270289308328347366203842VHL_A13813EGJ_A203861O12_A13816JKU_A503831YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 1.01e-78 20 384 24 388
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]
3EGJ_A 5.28e-60 1 381 4 377
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]
1O12_A 1.40e-58 20 386 32 375
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]
6JKU_A 3.18e-58 1 381 18 391
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 7.37e-56 50 383 51 379
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 Snap193857779611513515417319321223125027028930832834736620384sp|O34450|NAGA_BACSU20370sp|Q84F86|NAGA_LYSSH1381sp|O32445|NAGA_VIBCH50386sp|P96166|NAGA_VIBFU4386sp|P34480|NAGA_CAEEL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 5.52e-78 20 384 24 388
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 3.49e-70 20 370 25 369
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O32445 2.67e-59 1 381 1 374
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nagA PE=1 SV=2
P96166 2.51e-58 50 386 57 388
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
P34480 7.89e-58 4 386 23 416
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
1.000051 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000391_00114.