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CAZyme Information: MGYG000002178_00115

You are here: Home > Sequence: MGYG000002178_00115

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-617;
CAZyme ID MGYG000002178_00115
CAZy Family CE9
CAZyme Description N-acetylglucosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000002178_3|CGC1 42133.38 5.6742
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002178 2197502 MAG Spain Europe
Gene Location Start: 39545;  End: 40705  Strand: +

Full Sequence      Download help

MLKQIVNGRI  LTPEGWLRDG  SVIIEGNKIL  EVSNCHLPVV  GAEIIDAHGC  DVVPGGIEMH60
VHGGGGRDFM  EGTEDAFRTA  VDAHMQHGTT  AIFPTLSSST  MPMIRAAVAT  TEKLMAEPDS120
PVMGLHLEGH  YLSLEMAGGQ  IPENIKNPDP  AEYEPLLSST  RCIKRWDAAP  ELPGIREFGA180
CCVRHGVLPS  VAHTAAEYPD  VKAAYEAGFT  HATHFYNAMK  GFHKVREYKH  EGTVESVYAL240
PDMTVEMIAD  GIHVPPVILR  MIYLVKGVER  TAMITDALAC  AASDSQTAFD  PRVIIEDGVC300
KLSDRSALAG  SIATMDRLVR  TAVQQAGIPM  EDACRMVSET  PARIMHIYDR  KGSLQRGKDA360
DIILFDSDQQ  LRFVMQMGRV  VRNELS386

Enzyme Prediction      help

No EC number prediction in MGYG000002178_00115.

CAZyme Signature Domains help

Created with Snap19385777961151351541731932122312502702893083283473665378CE9
Family Start End Evalue family coverage
CE9 5 378 3.1e-104 0.9973190348525469

CDD Domains      download full data without filtering help

Created with Snap19385777961151351541731932122312502702893083283473665378NagA5381NagA5379nagA7368nagA52374Amidohydro_1
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 1.57e-129 5 378 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 5.63e-110 5 381 4 378
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 4.91e-77 5 379 7 380
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 2.37e-56 7 368 6 366
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 5.11e-21 52 374 2 317
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 Snap19385777961151351541731932122312502702893083283473661381QUT49240.1|CE91381QRP58027.1|CE91381AAO75782.1|CE91381QUU09057.1|CE91381QMW87717.1|CE9
Hit ID E-Value Query Start Query End Hit Start Hit End
QUT49240.1 6.29e-213 1 381 1 381
QRP58027.1 2.43e-210 1 381 1 381
AAO75782.1 2.43e-210 1 381 1 381
QUU09057.1 2.43e-210 1 381 1 381
QMW87717.1 2.43e-210 1 381 1 381

PDB Hits      download full data without filtering help

Created with Snap1938577796115135154173193212231250270289308328347366103816FV3_A103816FV4_A53833EGJ_A103802VHL_A53811YMY_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FV3_A 2.66e-46 10 381 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]
6FV4_A 3.85e-45 10 381 24 392
Thestructure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155],6FV4_B The structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D267A mutant from Mycobacterium smegmatis in complex with N-acetyl-D-glucosamine-6-phosphate [Mycolicibacterium smegmatis MC2 155]
3EGJ_A 9.52e-45 5 383 7 381
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]
2VHL_A 1.04e-35 10 380 12 386
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]
1YMY_A 1.55e-35 5 381 4 379
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 Snap19385777961151351541731932122312502702893083283473665383sp|O32445|NAGA_VIBCH1383sp|P44537|NAGA_HAEIN9381sp|P96166|NAGA_VIBFU10380sp|O34450|NAGA_BACSU5381sp|P0AF18|NAGA_ECOLI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
O32445 4.88e-44 5 383 4 378
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
P44537 1.58e-39 1 383 1 381
N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA PE=3 SV=1
P96166 1.18e-36 9 381 14 385
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O34450 5.69e-35 10 380 12 386
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P0AF18 8.51e-35 5 381 4 379
N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002178_00115.