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CAZyme Information: MGYG000002329_00463

You are here: Home > Sequence: MGYG000002329_00463

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 Dielma sp001305055
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Dielma; Dielma sp001305055
CAZyme ID MGYG000002329_00463
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
393 MGYG000002329_2|CGC4 43340.79 5.6011
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002329 3357599 Isolate not provided not provided
Gene Location Start: 168086;  End: 169267  Strand: +

Full Sequence      Download help

MIIKCKRIVT  EDGIIDGYLE  IEGKKIKRIT  KREIGSVDVD  ASQYRIIPGI  FDTHNHGTMG60
YAMMSAVSDD  EANVRGYLKG  LASQGVTSIL  PTAEFELFPV  IAKVSKEDND  GAKIIGIHSE120
GPYLNRVGEK  AIDTGHPDIR  LDHLQAMIDA  ADGTLKLVGL  APELENADKA  IEFLTERGIR180
VAFTHSNCNY  DEAIAAFRKG  ITVTTHTANV  MSGIHHRRMG  GLGACLLDPY  VNNEIICDLL240
HVSKEMLQIM  FKCKPYDKFM  MISDNVPMAG  APIGRYMIDK  DLAVNIDEKG  YCLTDTGRLC300
GSTKPVLFGI  RNLVEELELP  LETVSKMASL  NPCRVYGIGD  TKGSLRAGKD  ADFVIISDDY360
QALQTYSEGR  KVYDHEIDTH  IFNQAFLDVM  SAK393

Enzyme Prediction      help

No EC number prediction in MGYG000002329_00463.

CAZyme Signature Domains help

Created with Snap19395878981171371571761962162352552752943143343533734369CE9
Family Start End Evalue family coverage
CE9 4 369 1.7e-91 0.9946380697050938

CDD Domains      download full data without filtering help

Created with Snap19395878981171371571761962162352552752943143343533731369NagA1374NagA3370nagA7365nagA46362Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 2.10e-95 1 369 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 6.48e-89 1 374 2 380
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.05e-56 3 370 7 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 1.53e-30 7 365 8 372
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 2.77e-11 46 362 2 314
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 Snap19395878981171371571761962162352552752943143343533731388BBB48842.1|CE97388QIA42332.1|CE97388ATO99271.1|CE91386QIK57080.1|CE93389AOT69371.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
BBB48842.1 1.43e-138 1 388 1 389
QIA42332.1 1.82e-134 7 388 7 394
ATO99271.1 1.82e-134 7 388 7 394
QIK57080.1 1.05e-131 1 386 1 383
AOT69371.1 1.42e-111 3 389 5 395

PDB Hits      download full data without filtering help

Created with Snap1939587898117137157176196216235255275294314334353373123731O12_A23737NUT_A13702VHL_A53703EGJ_A483721YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1O12_A 8.38e-38 12 373 25 373
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]
7NUT_A 3.86e-34 2 373 20 402
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]
2VHL_A 2.10e-32 1 370 5 385
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 3.02e-31 5 370 10 377
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]
1YMY_A 5.84e-31 48 372 53 379
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 Snap19395878981171371571761962162352552752943143343533739374sp|P96166|NAGA_VIBFU2370sp|Q8XAC3|AGAA_ECO578376sp|Q8JZV7|NAGA_MOUSE8376sp|Q5BJY6|NAGA_RAT8376sp|A7MBC0|NAGA_BOVIN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P96166 7.83e-48 9 374 29 387
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3 1.67e-40 2 370 4 373
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q8JZV7 8.51e-37 8 376 26 405
N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
Q5BJY6 1.18e-36 8 376 26 405
N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
A7MBC0 4.28e-35 8 376 26 405
N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 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
1.000037 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002329_00463.