CAZyme Information: MGYG000000572_00246

Basic Information

• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1
• CAZyme ID: MGYG000000572_00246
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
321		35285.61	5.996

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000572	1867050	MAG	Madagascar	Africa

• Gene Location: Start: 7517; End: 8482 Strand: -

Full Sequence      

MQTKLIIEQHFHGCFGIDFNKASVDDVLYLSKEILKYGIGGIFPTLVTDSVENIRKATAI
IREACAKQTPDMAKILGIHLEGIFINPEKKGIHNPEHFLAPTIENYKLVEDDFIKIVTLA
PELIPDAKTQIGEDAKSVSENGNLISYLRFKNIKVQAGHCVGGDLDGCTGVTHLFNAMSG
VVHRGETTALSALVNDDIYTEIIGDGIHVSDKALKLVFKSKPLDKILLISDSLPITGSNL
KEMIFADEKVYYDGIKATSKEGTIAGSTTMIPKIIKRLAKAGIIAENEINQIINNTYNYH
NVNIDGSISWDEDFNIIKVSK

Enzyme Prediction     

No EC number prediction in MGYG000000572_00246.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	7	286	3.6e-65	0.7319034852546917

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	3.98e-76	7	319	54	370	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	2.09e-69	7	319	55	371	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	2.24e-59	6	321	58	368	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	3.06e-40	7	283	56	326	N-acetylglucosamine-6-phosphate deacetylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOR38279.1	2.31e-184	1	321	1	348
AQR97681.1	2.39e-44	7	319	52	368
AGF59010.1	1.91e-42	7	319	52	368
ARC85415.1	3.90e-42	7	278	57	318
ACK41552.1	1.43e-41	7	283	56	324

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YMY_A	3.63e-34	7	283	56	326	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]
2P53_A	1.88e-33	7	283	56	326	ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
2VHL_A	1.18e-30	6	267	59	317	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]
3EGJ_A	2.50e-30	7	283	59	326	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	4.88e-26	3	283	69	340	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
P0AF19	1.99e-33	7	283	56	326	N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=nagA PE=2 SV=1
P0AF18	1.99e-33	7	283	56	326	N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1
O34450	6.46e-30	6	267	59	317	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
O32445	1.31e-29	7	283	56	323	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
P44537	8.58e-26	3	276	53	318	N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA 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
1.000049	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000572_00246.