dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000280_00014

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Basic Information help

Species

AM51-8 sp003478275

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; AM51-8; AM51-8 sp003478275

CAZyme ID

MGYG000000280_00014

CAZy Family

CE9

CAZyme Description

N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
385	MGYG000000280_1\|CGC1	41519.08	5.0124

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000280	2599910	Isolate	China	Asia

Gene Location

Start: 6264; End: 7421 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000280_00014.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	3	384	2.5e-115	0.9865951742627346

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	2.25e-124	1	385	1	371	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	6.68e-107	1	382	2	369	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	4.65e-79	3	381	7	372	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	1.05e-57	5	372	6	360	N-acetylglucosamine-6-phosphate deacetylase; Provisional
COG1228	HutI	1.81e-23	1	376	12	374	Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL22760.1	2.36e-128	1	385	1	366
QIB56106.1	6.48e-126	1	385	1	367
QMW81160.1	6.48e-126	1	385	1	367
QBE96063.1	1.85e-125	1	385	1	367
AWY96831.1	4.25e-124	1	385	1	367

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	4.95e-61	1	381	5	377	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	7.44e-49	17	382	28	392	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]
1YMY_A	2.29e-47	3	385	4	373	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	1.22e-46	3	385	4	373	ChainA, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
3EGJ_A	1.42e-41	3	382	7	370	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34450	2.71e-60	1	381	5	377	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
Q6P0U0	3.30e-50	11	382	22	392	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
A7MBC0	5.18e-50	17	382	28	392	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q5BJY6	1.49e-48	17	382	28	392	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
Q8JZV7	4.08e-48	17	382	28	392	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000280_00014.