CAZyme Information: MGYG000001731_00114

Basic Information

• Species: Collinsella sp900751665
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900751665
• CAZyme ID: MGYG000001731_00114
• CAZy Family: CE9
• CAZyme Description: N-acetylgalactosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
218	MGYG000001731_4|CGC1	22700.63	4.8421

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001731	1951311	MAG	Sweden	Europe

• Gene Location: Start: 15898; End: 16554 Strand: +

Full Sequence      

MAAERDGAAAYAAALNAKGVVTSIGHSDATYDECIAAINAGASCFTHTYNGQRGLHHREP
GVVGAAMSTPETYAEIICDGKHVNPAAIKALLQAKGWQHTVLITDCLGCGGMPEGSYTSG
GMDVIMKDNLCWLADGKSIAGSVLTLAQGVKNIVDWGIASADIAIRMATEVPARSAHIED
KCGSIMPGRDADFVVFDHELTLVETYVGGQSVGNAFTE

Enzyme Prediction     

No EC number prediction in MGYG000001731_00114.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	1	209	1.3e-75	0.5549597855227882

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	2.26e-88	1	209	167	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	5.50e-82	2	210	169	376	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	1.46e-52	1	210	172	380	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	5.29e-44	18	214	187	381	N-acetylglucosamine-6-phosphate deacetylase; Provisional
cd01308	Isoaspartyl-dipeptidase	1.10e-08	140	210	303	372	Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA33930.1	4.41e-157	1	218	172	389
ATP54175.1	4.41e-157	1	218	172	389
AZH70255.1	7.27e-156	1	218	172	389
ATP54184.1	8.36e-148	1	218	172	389
BBH50707.1	2.01e-113	1	214	173	390

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3EGJ_A	1.10e-34	19	210	188	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]
2VHL_A	1.48e-32	15	209	191	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]
6FV3_A	1.60e-32	1	212	179	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	2.25e-31	1	212	179	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]
1YMY_A	6.52e-30	19	212	188	379	CrystalStructure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YMY_B Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YRR_A Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],1YRR_B Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],2P50_A Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_B Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_C Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_D Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96166	3.20e-45	1	217	176	390	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3	4.61e-38	1	210	166	373	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q84F86	6.40e-35	1	210	173	380	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O32445	5.72e-34	19	210	185	374	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nagA PE=1 SV=2
P42906	6.60e-32	47	210	2	163	Putative N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=agaA PE=5 SV=3

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
0.999863	0.000188	0.000002	0.000001	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001731_00114.