logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000249_00234

You are here: Home > Sequence: MGYG000000249_00234

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 Mediterraneibacter faecis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter faecis
CAZyme ID MGYG000000249_00234
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
374 MGYG000000249_1|CGC4 40620.09 4.6875
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000249 3112009 Isolate China Asia
Gene Location Start: 262126;  End: 263250  Strand: -

Full Sequence      Download help

MKLIKEKKIY  TGDGVIENGY  IRFDEKIEEV  GDMAGFEPKE  GDLEVSCAGT  MVVPGFIDIH60
SHGGYGKDNM  DATPDEIDEM  VKQMTKQEGI  TTYFCTTMTQ  TYENIEKAMQ  NIHDAAQKNP120
VIKGIHLEGP  FISTVFKGAQ  DPSYIKKPDE  KTLAKWNEIS  GGLLRIVTYA  PEEADPSFET180
WCRENGVVLS  AGHSNALYGE  LNASGATHVT  HLYNAQRGLN  HREPGVTGYG  MLAEGVHAEL240
ICDGKHIVPD  MVKLACKVRG  YDGIELITDS  MRAKGMPEGK  SELGGQVVIV  KDGMAKLEDG300
TIAGSILTYI  QAFKNVMEFT  GATVEDAVKM  TSGNQAKEFG  LDSKGAIAAG  KDADMVVLNE360
DFDLVQTISY  GKLA374

Enzyme Prediction      help

No EC number prediction in MGYG000000249_00234.

CAZyme Signature Domains help

Created with Snap18375674931121301491681872052242432612802993173363554370CE9
Family Start End Evalue family coverage
CE9 4 370 2.2e-119 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap18375674931121301491681872052242432612802993173363552371NagA1374NagA1372nagA8372nagA51373Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 6.64e-151 2 371 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 3.03e-139 1 374 1 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 3.97e-102 1 372 4 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 8.24e-55 8 372 8 377
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.20e-15 51 373 1 334
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 Snap18375674931121301491681872052242432612802993173363551374CBL24842.1|CE91372QRT31720.1|CE91373QHB25336.1|CE91373QEI32487.1|CE91373API88808.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
CBL24842.1 2.46e-270 1 374 1 374
QRT31720.1 1.13e-182 1 372 1 376
QHB25336.1 1.24e-179 1 373 1 377
QEI32487.1 1.24e-179 1 373 1 377
API88808.1 2.52e-157 1 373 2 374

PDB Hits      download full data without filtering help

Created with Snap183756749311213014916818720522424326128029931733635533742VHL_A103741O12_A83723EGJ_A33726FV3_A13721YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 1.57e-86 3 374 6 387
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 4.58e-71 10 374 28 372
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 1.27e-46 8 372 11 377
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]
6FV3_A 3.84e-46 3 372 18 390
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]
1YMY_A 9.71e-46 1 372 1 377
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 Snap18375674931121301491681872052242432612802993173363553374sp|O34450|NAGA_BACSU40373sp|Q84F86|NAGA_LYSSH3374sp|Q8XAC3|AGAA_ECO5727374sp|P96166|NAGA_VIBFU8372sp|O32445|NAGA_VIBCH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 8.59e-86 3 374 6 387
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 9.13e-77 40 373 42 381
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3 1.72e-51 3 374 4 375
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166 1.12e-50 27 374 29 385
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O32445 6.49e-46 8 372 8 374
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

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
1.000071 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000249_00234.