dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000271_01751

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Basic Information help

Species

Roseburia sp900552665

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900552665

CAZyme ID

MGYG000000271_01751

CAZy Family

CE9

CAZyme Description

N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
381	MGYG000000271_13\|CGC1	41629.66	5.1851

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000271	4008876	Isolate	China	Asia

Gene Location

Start: 29631; End: 30776 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000271_01751.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	6	376	1.3e-115	0.9946380697050938

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	2.69e-133	3	376	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	1.58e-120	4	381	3	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	4.29e-86	1	377	3	380	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	8.32e-53	7	377	6	377	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	1.42e-20	51	379	2	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
ASM68821.1	3.08e-178	1	381	1	384
AWY98752.1	4.75e-172	1	381	1	384
ANU48011.1	6.50e-172	1	376	1	377
QQR03992.1	3.26e-171	5	376	11	383
CBK80127.1	3.25e-166	1	379	18	404

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	3.14e-65	21	378	24	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	2.82e-51	21	381	32	374	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	3.89e-46	15	379	25	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]
6JKU_A	2.29e-43	6	376	22	390	Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_C Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_D Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida]
6FV3_A	2.66e-42	45	376	58	389	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

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34450	1.72e-64	21	378	24	386	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86	4.12e-59	23	364	27	367	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3	3.10e-55	21	378	22	374	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166	7.28e-50	51	379	57	385	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q6P0U0	1.76e-47	6	381	16	403	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 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
1.000085	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000271_01751.