dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002953_03048

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Basic Information help

Species

UMGS1202 sp900549565

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UMGS1202; UMGS1202 sp900549565

CAZyme ID

MGYG000002953_03048

CAZy Family

CE9

CAZyme Description

N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
387		40540.39	6.5655

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002953	3706118	MAG	United States	North America

Gene Location

Start: 8505; End: 9668 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002953_03048.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	10	380	9.3e-112	0.9892761394101877

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	7.00e-126	8	380	4	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	8.71e-110	8	385	5	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	3.42e-74	45	380	46	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	9.80e-45	17	380	15	376	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	8.65e-14	52	383	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

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU39739.1	9.67e-212	1	386	1	385
QQR07434.1	9.67e-212	1	386	1	385
QIA29312.1	1.31e-209	1	386	1	385
BBH49623.1	1.11e-190	1	386	4	389
ASM68821.1	8.75e-131	17	380	17	379

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	5.06e-57	23	384	24	388	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	2.91e-53	22	384	31	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	2.60e-51	11	387	19	405	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	2.27e-40	53	368	64	377	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	3.17e-39	53	368	64	377	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	2.67e-58	12	368	14	367	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O34450	2.77e-56	23	384	24	388	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0	2.64e-51	11	387	19	405	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q9Y303	1.42e-50	11	387	19	405	N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
Q5BJY6	3.07e-48	11	387	19	405	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 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
1.000078	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002953_03048.