CAZyme Information: MGYG000000095_03904

Basic Information

• Species: GCA-900066755 sp902363085
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066755; GCA-900066755 sp902363085
• CAZyme ID: MGYG000000095_03904
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
383	MGYG000000095_15|CGC1	42122.19	5.6696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000095	5524222	Isolate	United Kingdom	Europe

• Gene Location: Start: 47872; End: 49023 Strand: -

Full Sequence      

MEIIHVNILEDGEILENFFIRTRNGLIQDIDTMEHYRRIQEEVLDGEHQFLCPGFIDIHN
HGAVGFDAMDGTAEALAGIAGFHFQNGVTSFLATTMTAPLKQVKKLADLLEGGLKTDADI
LGIHMEGPFLSERNKGAQPGQYLLRPQEEHFRILDEMKPWIRLITVSPDVPHIGLLLKYC
RVNGITVSGGHDGAIDEEIYRAVEGGMKSVTHLYCCSSSISRRQDAVKHIGLTEIGLEDD
RLYAEVVADGHHIPAALFRLIYKCKGYRKICLVSDEIRAAGLGEGEFMLGSGEHGVPVTV
TDGIALLKSENVYAGSVTPISRMVEQLTASGAVPIGQACYMASSAPAELLGLRDRGHIRE
GCAAHFNILDREGRLRRTIKEEI

Enzyme Prediction     

No EC number prediction in MGYG000000095_03904.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	5	380	8.3e-94	0.9865951742627346

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	2.22e-104	3	381	2	373	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	3.27e-91	3	381	4	374	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	1.64e-55	3	379	7	376	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	1.53e-30	13	379	14	373	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	2.62e-12	50	370	1	309	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQO09505.1	2.76e-116	1	382	2	385
BCJ98632.1	2.19e-72	1	379	4	384
AYO31105.1	3.58e-69	8	370	4	384
QEC79978.1	1.39e-65	43	379	45	384
ASZ14075.1	1.47e-65	1	370	5	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1O12_A	3.39e-40	51	381	53	368	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	5.11e-37	6	355	10	356	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]
7NUT_A	2.21e-33	1	370	13	386	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	4.48e-30	51	372	64	379	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	5.78e-29	51	372	64	379	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96166	3.97e-41	24	353	32	352	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q84F86	3.18e-40	16	380	21	377	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
Q8XAC3	1.41e-36	15	370	17	360	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O34450	2.80e-36	6	355	10	356	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0	6.68e-35	8	378	20	394	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000041	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000095_03904.