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CAZyme Information: MGYG000001383_00647

You are here: Home > Sequence: MGYG000001383_00647

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 Lactobacillus iners
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus iners
CAZyme ID MGYG000001383_00647
CAZy Family CE9
CAZyme Description N-acetylgalactosamine-6-phosphate deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000001383_1|CGC6 42384.47 6.2237
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001383 1269142 Isolate not provided not provided
Gene Location Start: 678285;  End: 679445  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001383_00647.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE9 7 379 5e-116 0.9919571045576407

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00854 NagA 4.22e-154 11 379 8 374
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 2.70e-129 3 379 2 375
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221 nagA 1.39e-76 1 379 3 379
N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170 nagA 4.87e-51 35 379 33 376
N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979 Amidohydro_1 1.16e-11 52 370 1 312
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

Hit ID E-Value Query Start Query End Hit Start Hit End
QIH24316.1 2.75e-289 1 386 1 386
QIH25643.1 3.90e-289 1 386 1 386
QIH28151.1 5.54e-289 1 386 1 386
QIH26965.1 5.54e-289 1 386 1 386
QIC18869.1 1.59e-288 1 386 1 386

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHL_A 6.04e-54 13 379 15 384
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 3.47e-42 52 379 52 369
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]
6FV3_A 1.13e-41 20 372 34 382
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 1.59e-40 20 372 34 382
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]
7NUT_A 1.34e-39 46 379 56 398
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8XAC3 7.04e-67 37 379 31 372
N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166 1.09e-64 55 379 59 382
N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O34450 3.31e-53 13 379 15 384
N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86 3.98e-52 47 386 48 386
N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q9VR81 2.24e-41 52 384 76 414
N-acetylglucosamine-6-phosphate deacetylase OS=Drosophila melanogaster OX=7227 GN=CG17065 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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001383_00647.