CAZyme Information: MGYG000000079_00104

Basic Information

• Species: Exiguobacterium sp902362975
• Lineage: Bacteria; Firmicutes; Bacilli; Exiguobacterales; Exiguobacteraceae; Exiguobacterium; Exiguobacterium sp902362975
• CAZyme ID: MGYG000000079_00104
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382	MGYG000000079_1|CGC1	41770.99	4.8515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000079	2825544	Isolate	United Kingdom	Europe

• Gene Location: Start: 96057; End: 97205 Strand: +

Full Sequence      

MGTLINARIVSAEHTWEHGYIRWNGQTIDEIGSMEQFEQQDEHVIDVAGALVTPGLIDVH
IHGGYEVDTMDADESKLRQLSNDMLQEGVTSFFATTITQSKEAIEHALKAVRNVIEAQDT
TLIGIHLEGPFVNVEMAGAQPAEYIIDPDAEQFRKWQELAGGHIRLVTYAPERPGARAFE
SVLRETGAIGSAGHTSATFEENKQAGVKHGTHLYNQMRGLHHREPGTVGYCLLEGGVIAE
IIPDGIHSRPEMVDFAFRLKGADELVVITDAMRAKGLPDGQYELGGQPVIVADGAARLKA
GNLAGSVLTMDAAFRNIQAYTGCTVEEAVKMTSTNAAKEFGLTTKGDIKSGFDADLVVWD
DTTHVQMTFVKGRIVYKREEQR

Enzyme Prediction     

No EC number prediction in MGYG000000079_00104.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	5	372	5.9e-132	0.9946380697050938

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	1.22e-160	3	372	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	5.07e-147	1	376	1	379	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	6.90e-107	4	373	7	380	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	8.16e-56	1	375	1	379	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	1.07e-22	51	375	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACQ71176.1	7.41e-276	1	382	1	382
QPI67249.1	1.01e-273	1	382	1	382
QUP86704.1	1.18e-272	1	382	1	382
QUE86252.1	3.21e-208	1	380	1	380
QWB30605.1	1.67e-166	1	372	1	372

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	4.46e-94	9	380	12	392	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	1.92e-61	51	377	52	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	4.93e-49	46	382	57	408	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	2.50e-45	46	375	58	392	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	3.60e-44	46	375	58	392	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
Q84F86	1.93e-101	45	374	47	381	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O34450	2.44e-93	9	380	12	392	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P96166	6.20e-58	27	376	28	386	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3	6.76e-54	51	374	46	374	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
A7MBC0	2.05e-53	46	382	57	408	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	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000079_00104.