dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000437_01421

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Basic Information help

Species

Alistipes sp001941065

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065

CAZyme ID

MGYG000000437_01421

CAZy Family

CE9

CAZyme Description

N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389	MGYG000000437_45\|CGC1	42227.77	5.0625

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000437	3341375	MAG	Sweden	Europe

Gene Location

Start: 18495; End: 19664 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000437_01421.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	6	385	8.1e-114	0.9946380697050938

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	2.82e-147	4	385	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	6.44e-117	4	389	3	379	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	5.91e-85	1	385	3	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	4.24e-53	45	386	45	377	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	2.00e-23	50	387	1	334	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
BCG54161.1	3.90e-174	2	386	3	390
SCM56970.1	8.33e-164	1	389	1	393
BBD44964.1	7.03e-163	5	389	7	394
SCD19170.1	8.12e-162	38	389	43	394
SCM59668.1	4.13e-157	42	385	47	390

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FV3_A	3.85e-47	19	386	34	390	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	5.59e-46	19	386	34	390	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	1.90e-43	40	386	52	399	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]
1O12_A	2.59e-43	51	389	53	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]
2VHL_A	3.95e-43	19	389	22	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	1.26e-50	25	388	29	382	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3	3.22e-47	24	386	25	373	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166	7.98e-45	25	389	32	386	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
A7MBC0	2.68e-44	40	386	52	399	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q5BJY6	7.28e-44	40	386	52	399	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
1.000075	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000437_01421.