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CAZyme Information: MGYG000000037_01141

You are here: Home > Sequence: MGYG000000037_01141

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 Turicibacter sp001543345
Lineage Bacteria; Firmicutes; Bacilli; Haloplasmatales_A; Turicibacteraceae; Turicibacter; Turicibacter sp001543345
CAZyme ID MGYG000000037_01141
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
378 MGYG000000037_13|CGC1 41385.32 4.9266
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000037 2730783 Isolate United Kingdom Europe
Gene Location Start: 28094;  End: 29230  Strand: +

Full Sequence      Download help

MKAIINGKLV  TLNGVIENKV  LVFNETIQHI  QTEVPIDCEV  IDAKGMYIAP  GLIDVHVHGS60
CGADTMDQTT  EAIKLMGTGI  AKNGVTSFLP  TTMTMSPKDI  YGALNVIREC  MEQSLNGAKV120
LGAHMEGPFI  NRIYKGAQPE  QYVIKPSYEF  IKDYTDVIRL  VSYAPEMDED  YSFTKDVKEK180
TDITLSIGHT  NATYDQAKEA  FSLGCSHVTH  LFNAMTPLNH  REPGVVGASL  TSDVFTELIA240
DTIHVNKQLF  QFVLDNKGKE  KIVLITDSMR  GGCMKEGQYD  LGGQRVVVKD  GAARLESGNL300
AGSVLTLNKA  IYNFLQNTNA  TIAEVIHMAS  LNPATSIGVC  NRKGSLEIGK  DADIAIFDEE360
MNCYLSIVEG  REVYNQLD378

Enzyme Prediction      help

No EC number prediction in MGYG000000037_01141.

CAZyme Signature Domains help

Created with Snap18375675941131321511701892072262452642833023213403595369CE9
Family Start End Evalue family coverage
CE9 5 369 6.4e-125 0.9919571045576407

CDD Domains      download full data without filtering help

Created with Snap18375675941131321511701892072262452642833023213403592370NagA1375NagA1371nagA1376nagA47358Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 2.22e-159 2 370 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 3.79e-147 1 375 1 380
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.33e-107 1 371 4 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 5.53e-84 1 376 1 382
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.56e-22 47 358 1 309
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 Snap18375675941131321511701892072262452642833023213403591378AMC08720.1|CE91377QJS18904.1|CE91377AJF28709.1|CE91377AJF31770.1|CE91377ACD51050.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
AMC08720.1 4.27e-273 1 378 1 378
QJS18904.1 2.35e-215 1 377 1 377
AJF28709.1 6.86e-189 1 377 1 377
AJF31770.1 6.86e-189 1 377 1 377
ACD51050.1 6.86e-189 1 377 1 377

PDB Hits      download full data without filtering help

Created with Snap183756759411313215117018920722624526428330232134035993712VHL_A13753EGJ_A483741O12_A333761YMY_A333762P53_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 2.50e-80 9 371 12 385
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 6.43e-63 1 375 4 381
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 1.70e-57 48 374 53 373
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 4.53e-55 33 376 36 382
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 2.47e-54 33 376 36 382
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Created with Snap18375675941131321511701892072262452642833023213403599371sp|O34450|NAGA_BACSU28371sp|Q84F86|NAGA_LYSSH35371sp|Q8XAC3|AGAA_ECO571375sp|O32445|NAGA_VIBCH48375sp|P96166|NAGA_VIBFU
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 1.37e-79 9 371 12 385
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 2.91e-76 28 371 37 380
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3 2.89e-63 35 371 34 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O32445 3.25e-62 1 375 1 378
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 5.13e-59 48 375 57 387
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD 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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000037_01141.