CAZyme Information: MGYG000003529_00136

Basic Information

• Species: SFLA01 sp004553575
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-382; SFLA01; SFLA01 sp004553575
• CAZyme ID: MGYG000003529_00136
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366		38752.16	5.4206

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003529	1658319	MAG	Fiji	Oceania

• Gene Location: Start: 17757; End: 18857 Strand: -

Full Sequence      

MRIYGGTVFCPDRIMRQTDVCFYDGRITADSDTGGFDASDCYVLPGFIDTHIHGAFGSEF
SSPDEDFTPALDSLSKRGVTSVLATTRSLFPDELEAAARNIGRQADPRVIGIHAEGPFVN
PARIGAMNPKKLSLPKVSIPETMNSVSGGKLKILSMAPELDGAGEVIDWCVANGVKVSMA
HTDADCASARAAVDRGASRLTHTYNGMRPLHHREPGVLGEALTDDRVCCELICDLVHVSA
PAISLAVRAKGAENITMVSDSGVFSGLGDGEYTVDGRKRIVKDGVCRCADGVTIAGSTKC
LYDGVLNMFRLGYSPDKIAIMASVNPALACGCTDRGILAEGCRADIAVLDRDFGIKAVFV
GGERVV

Enzyme Prediction     

No EC number prediction in MGYG000003529_00136.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	5	362	4.6e-105	0.9919571045576407

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	5.87e-115	1	362	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	5.91e-100	3	366	4	379	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	3.27e-70	37	362	48	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	2.31e-40	45	366	53	380	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	1.17e-17	42	365	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
AYO31542.1	4.82e-72	8	365	10	394
QAT60739.1	5.43e-72	1	362	3	383
AST56602.1	2.64e-71	6	365	9	379
QSQ08626.1	8.19e-71	3	364	5	391
AIS51397.1	2.45e-70	6	365	9	380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FV3_A	1.83e-50	43	366	64	393	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	2.71e-49	43	366	64	393	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]
1O12_A	4.21e-49	43	365	53	372	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	6.65e-49	39	352	51	374	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	1.18e-39	3	365	33	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	1.76e-51	17	363	22	380	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O34450	3.64e-48	39	352	51	374	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q8XAC3	1.35e-46	43	363	47	373	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
A7MBC0	8.28e-43	3	365	33	401	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
P96166	1.84e-42	23	365	41	385	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 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
0.999979	0.000080	0.000004	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003529_00136.