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CAZyme Information: MGYG000000727_00565

You are here: Home > Sequence: MGYG000000727_00565

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; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; SFFS01;
CAZyme ID MGYG000000727_00565
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
382 MGYG000000727_5|CGC1 40685.56 5.4091
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000727 2530364 MAG Kazakhstan Asia
Gene Location Start: 15416;  End: 16564  Strand: -

Full Sequence      Download help

MQAILNGRIL  MPDGVVTGRA  LLFEERIIGL  CAPDALPEKC  EVIDAGGQYV  APGLIDLHIH60
GYMGEDASDA  SAEGVRIMAR  GIARNGVTSW  LPTTMTVSKQ  QLCAAFDNIR  TLRQESRTAA120
WDGAEILGVN  AEGPFINPAR  KGAQNGEHVL  LPDPGFLLDF  ADVVRITTLA  PEMEGGLAFI180
DAVKAKSDIL  ISMGHTDATF  EQAKEAVAHG  LGHATHTFNA  MTGLNHRAPG  VAGAALTLPV240
TAELIADTFH  IHPGLFPLMV  KAKGDKLCLI  TDCTRAGGLS  DGEYSLGGQP  IFVRGIECRL300
ADGTIAGSVL  KLNRAVKNLV  DYTGLPVYEA  VNCASRNPAN  AIGQRNKGTL  ESGRDADIFL360
CNDDFEVSRT  ILRGKTIFME  ER382

Enzyme Prediction      help

No EC number prediction in MGYG000000727_00565.

CAZyme Signature Domains help

Created with Snap19385776951141331521711912102292482672863053243433625374CE9
Family Start End Evalue family coverage
CE9 5 374 1.8e-118 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap19385776951141331521711912102292482672863053243433623374NagA1378NagA1375nagA1375nagA49377Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.28e-145 3 374 2 374
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 4.03e-133 1 378 1 379
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 2.42e-99 1 375 4 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 1.33e-81 1 375 1 377
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 7.24e-19 49 377 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 Snap19385776951141331521711912102292482672863053243433621374SIP63105.1|CE91381QEK21509.1|CE91378QQQ87039.1|CE91378AWH76701.1|CE91378AXU49263.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
SIP63105.1 1.94e-135 1 374 1 376
QEK21509.1 1.32e-124 1 381 1 377
QQQ87039.1 3.77e-124 1 378 1 374
AWH76701.1 3.44e-117 1 378 1 374
AXU49263.1 3.44e-117 1 378 1 374

PDB Hits      download full data without filtering help

Created with Snap1938577695114133152171191210229248267286305324343362373812VHL_A13771YMY_A13772P53_A13753EGJ_A13756JKU_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 7.97e-70 37 381 42 391
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]
1YMY_A 5.25e-59 1 377 1 379
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 2.88e-58 1 377 1 379
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
3EGJ_A 2.16e-57 1 375 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]
6JKU_A 6.48e-56 1 375 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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap193857769511413315217119121022924826728630532434336237381sp|O34450|NAGA_BACSU43375sp|Q84F86|NAGA_LYSSH2378sp|P96166|NAGA_VIBFU1377sp|P0AF18|NAGA_ECOLI1377sp|P0AF19|NAGA_ECO57
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 4.37e-69 37 381 42 391
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 5.83e-67 43 375 47 380
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166 1.05e-59 2 378 13 386
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
P0AF18 2.87e-58 1 377 1 379
N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1
P0AF19 2.87e-58 1 377 1 379
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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000727_00565.