CAZyme Information: MGYG000004786_01854

Basic Information

• Species: Firm-11 sp900550955
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900550955
• CAZyme ID: MGYG000004786_01854
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
384		41031.96	6.0853

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004786	2686597	MAG	Denmark	Europe

• Gene Location: Start: 5918; End: 7072 Strand: +

Full Sequence      

MERLLLRGGEVYQDGRFVRADVLCEDGRVARVGENLPQDGARAMDMTGLRVAPGFIDAHT
HGAAGVDVNAADEEGLRRIAAFFATQGTTAFCASVLTDTEETTRRCLAHIQTVMDDRGRG
AQLLGAHLEGPFLAKEYKGAMPEHLLKEGDAALLRRYQEAFPGVVKYVTVSPEVPGVPEM
IAQIAEDVVVAIGHSGADYAASMRAIENGARCVTHTFNAMRLFHQHEPAIMGAALESDCY
CEAICDGRHLHPGTVRMLIKCKGWDRVMAVTDSIMAAGLPDGRYKLGVNDVVVEDGDAKL
ATTGVRAGSTLTTGQALQNLVKFTGHPVEDVLPLLTQNPARALRIDGRKGRIAPGMDADM
VALTKGLAVRSTIVGGVCVYEGIA

Enzyme Prediction     

No EC number prediction in MGYG000004786_01854.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	8	376	9.2e-121	0.9919571045576407

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	9.34e-135	4	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	3.52e-118	5	381	3	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	5.19e-77	2	376	3	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	2.40e-54	22	376	21	376	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	1.09e-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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK80127.1	2.98e-143	3	376	19	401
ANU48011.1	1.02e-142	3	381	2	382
QQR03992.1	1.26e-142	3	381	8	388
BBH49623.1	4.61e-141	6	380	10	387
ASM68821.1	6.82e-137	12	376	13	379

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	3.10e-53	2	376	3	384	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	7.58e-48	5	381	20	403	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	1.30e-46	28	376	42	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]
6FV4_A	1.88e-45	28	376	42	389	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	2.98e-45	14	381	25	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	2.09e-60	11	376	14	379	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
P96166	5.41e-56	9	381	18	387	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
O34450	1.70e-52	2	376	3	384	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q8XAC3	1.15e-51	51	376	47	372	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q9VR81	5.73e-51	13	381	36	414	N-acetylglucosamine-6-phosphate deacetylase OS=Drosophila melanogaster OX=7227 GN=CG17065 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
1.000044	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004786_01854.