CAZyme Information: MGYG000002204_01353

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-138; UBA5394
• CAZyme ID: MGYG000002204_01353
• CAZy Family: CE9
• CAZyme Description: N-acetylgalactosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
170		18313.11	5.6391

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002204	1445261	MAG	Spain	Europe

• Gene Location: Start: 48; End: 560 Strand: +

Full Sequence      

MGLFHQHRPGIMGAVLERDVYCEAICDGRHLHPGSVRMLLACKGYDRVVAITDSIQAAGL
PDGRYKLGVNDVVVVDGDAKLADTGVRAGSTLTMDQALKNLVRFTGQPVERILPLLTLQP
AKVIGMDQEKGSIAPGKDGDLVVLNDALDVMETYIAGVRVYAGKEKQEEN

Enzyme Prediction     

No EC number prediction in MGYG000002204_01353.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	1	157	1.7e-51	0.41823056300268097

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	1.30e-56	1	157	218	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	9.62e-51	1	162	219	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
PRK11170	nagA	1.28e-22	9	157	229	376	N-acetylglucosamine-6-phosphate deacetylase; Provisional
PRK10657	PRK10657	9.36e-11	84	165	300	380	isoaspartyl dipeptidase; Provisional
cd01309	Met_dep_hydrolase_C	1.61e-09	106	161	299	359	Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASM68821.1	7.26e-69	1	160	223	382
AWY98752.1	1.75e-68	1	169	223	387
CBK80127.1	5.08e-68	1	160	246	404
ANU48011.1	6.14e-63	1	161	220	381
QQR03992.1	7.16e-63	1	161	226	387

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	4.73e-26	1	168	228	395	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	1.39e-24	4	161	240	402	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]
1O12_A	2.69e-24	5	164	218	376	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]
6JKU_A	7.07e-20	10	157	245	390	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]
1YMY_A	1.15e-18	9	160	229	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
P42906	2.88e-32	5	157	11	162	Putative N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=agaA PE=5 SV=3
Q8XAC3	2.69e-30	5	157	221	372	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
Q6P0U0	1.48e-26	4	161	240	402	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
O34450	2.59e-25	1	168	228	395	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0	1.09e-24	4	165	240	406	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
0.999964	0.000079	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002204_01353.