CAZyme Information: MGYG000002315_01420

Basic Information

• Species: Anaerococcus vaginalis_B
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus vaginalis_B
• CAZyme ID: MGYG000002315_01420
• CAZy Family: CE9
• CAZyme Description: N-acetylgalactosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
331		36034.34	5.2842

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002315	1997974	Isolate	France	Europe

• Gene Location: Start: 3959; End: 4954 Strand: -

Full Sequence      

MAPGLVDTHIHGYKNEDIMNAKKGALDIISQGLLECGVTSFLPTTLTDSTERLNEAVKVV
GEEYKDVKGAKVRGIFLEGPFFTEKYKGAQNEKYMSDPDIEKLKKWKELSKGLVNKIAIA
PERAGVEEFIKKANAMGVYVALGHSDASYDQAIKAVEDGANIFVHTFNAMSGLHHRNPGM
VGAAMNSDAISELICDGHHVNPAAAEILINKKGYDKIALITDCMMAGGMPDGSYKLGEFP
VKVEKGTARLESGNLAGSILKLKEAVQNVVDWDIVDIYEAVQMASLIPAKSVGIDDVCGK
IKVGYDADFILLDYELNLQKTFLNGEEKYRA

Enzyme Prediction     

No EC number prediction in MGYG000002315_01420.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	2	325	8.5e-120	0.871313672922252

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	4.65e-153	2	325	50	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	1.46e-145	2	330	51	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	5.11e-87	1	325	54	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	1.90e-52	1	328	51	379	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	5.96e-21	3	324	4	320	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
QQB61828.1	3.35e-225	1	330	45	374
QQN56511.1	9.59e-225	1	330	45	374
ACV28130.1	5.04e-183	1	329	45	374
QUY64861.1	2.91e-152	1	329	48	376
QZO77303.1	2.91e-152	1	329	48	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	5.30e-65	1	325	55	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]
1O12_A	8.16e-50	1	331	53	375	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	3.98e-46	1	331	63	404	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]
3EGJ_A	8.87e-45	1	326	54	377	N-acetylglucosamine-6-phosphatedeacetylase from Vibrio cholerae. [Vibrio cholerae],3EGJ_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae. [Vibrio cholerae],3IV8_A N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_B N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_C N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae],3IV8_D N-acetylglucosamine-6-phosphate deacetylase from Vibrio cholerae complexed with fructose 6-phosphate [Vibrio cholerae]
6JKU_A	4.97e-42	1	328	68	393	Crystalstructure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_C Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_D Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96166	5.03e-79	1	331	57	388	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3	3.24e-68	1	326	47	373	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
O34450	2.90e-64	1	325	55	384	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q84F86	9.01e-64	1	325	54	379	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
A7MBC0	7.15e-48	1	326	63	399	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
1.000059	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002315_01420.