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CAZyme Information: MGYG000002593_00571

You are here: Home > Sequence: MGYG000002593_00571

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 Limosilactobacillus sp900557215
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus sp900557215
CAZyme ID MGYG000002593_00571
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
378 MGYG000002593_5|CGC4 41661.11 5.5118
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002593 1475799 MAG China Asia
Gene Location Start: 54878;  End: 56014  Strand: +

Full Sequence      Download help

MQTVIKHADI  YTGEDTIKDG  YIRFTKSVLA  VGPMIEYQPE  ATDEQIIDGH  QTVIVPGFID60
VHSHGGYGID  TMDGDPDKLN  EMVHQVTKNE  GVTTFFPTTV  TQSVENINKA  MVAIKKAAAE120
NPVIQGTHLE  GPFVSAEYKG  AQPEKYIQDP  DYRLLDQWNE  LAGGLVKMIT  YAPEKPGAHE180
LEQYCLTHNI  VPSAGHSSAT  REQMKHSLAS  HITHLYNAQR  GMRHREPGLT  GDALMEDNLY240
TEIIADGFHV  VPDMIRLAYQ  IKGPDRMELI  TDSLRAKGMP  EGISELGGQK  VIVKDHQARL300
ENGHLAGSVL  QYNLAFQNII  DFTDCGIANA  VKMSSVNQAR  EFGLTTKGGL  TVGKDADLNI360
LDQNLNLKST  YSYGQLVK378

Enzyme Prediction      help

No EC number prediction in MGYG000002593_00571.

CAZyme Signature Domains help

Created with Snap18375675941131321511701892072262452642833023213403595373CE9
Family Start End Evalue family coverage
CE9 5 373 2.9e-120 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap183756759411313215117018920722624526428330232134035910374NagA3377NagA1370nagA7378nagA53377Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 8.94e-135 10 374 7 374
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 7.40e-126 3 377 2 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.65e-91 1 370 3 375
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.02e-44 7 378 6 380
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.29e-11 53 377 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 Snap18375675941131321511701892072262452642833023213403591378QCQ03433.1|CE91375QLL70791.1|CE91378SFV40208.1|CE91375QLE60793.1|CE91375QFR67817.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QCQ03433.1 1.66e-187 1 378 1 377
QLL70791.1 2.73e-187 1 375 1 375
SFV40208.1 3.35e-187 1 378 1 377
QLE60793.1 4.59e-187 1 375 1 373
QFR67817.1 4.59e-187 1 375 1 373

PDB Hits      download full data without filtering help

Created with Snap183756759411313215117018920722624526428330232134035943762VHL_A533771O12_A53753EGJ_A533777NUT_A103776FV3_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 5.66e-85 4 376 6 386
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 3.65e-64 53 377 52 372
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 1.87e-47 5 375 7 377
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]
7NUT_A 1.85e-46 53 377 62 401
ChainA, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUT_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_A Chain A, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens],7NUU_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Homo sapiens]
6FV3_A 8.88e-44 10 377 24 392
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]

Swiss-Prot Hits      download full data without filtering help

Created with Snap18375675941131321511701892072262452642833023213403594376sp|O34450|NAGA_BACSU47376sp|Q84F86|NAGA_LYSSH1376sp|Q8XAC3|AGAA_ECO5754377sp|P96166|NAGA_VIBFU47377sp|P34480|NAGA_CAEEL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34450 3.10e-84 4 376 6 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 3.31e-78 47 376 47 381
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3 9.53e-57 1 376 1 374
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166 9.02e-56 54 377 57 385
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
P34480 4.14e-48 47 377 64 413
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
1.000039 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002593_00571.