CAZyme Information: MGYG000000035_01637

Basic Information

• Species: Blautia_A hydrogenotrophica
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A hydrogenotrophica
• CAZyme ID: MGYG000000035_01637
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
367	MGYG000000035_3|CGC4	40235.97	5.4002

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000035	3529525	Isolate	United Kingdom	Europe

• Gene Location: Start: 409175; End: 410278 Strand: +

Full Sequence      

MIIKNGAVFQEDGLFKKQDLYIENHKIVASREEVSDDMEVDASGLLVIPGLIDIHSHGAA
GHDFSDGDAQGLKKILKYEKEHGITSYCPTSVTLPKERLKKIFATILEVEDYKEGATILG
INMEGPFIDPKKKGAHEESFIHKPSADFFKECNEACGNRIKLMTLAPNMEGGMKFIDEMH
NEVCISLGHTSMGYDTAAEAIERGAHHVTHLYNAMQPLAHRDPGLIGAAFDDRESMVELI
SDGFHIHPSVVRATFALFGPDRVILVSDSMMATGMPNGSYKLGDLNVTMKDRKATLEDGT
LAGSATDLYDCMRCAVSFGVPREHAIWAATRNPAKSIGIYDRVGSLTPGKEADVLLVDED
LKLCRVI

Enzyme Prediction     

No EC number prediction in MGYG000000035_01637.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	3	366	1.6e-127	0.9865951742627346

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	5.98e-138	1	367	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	2.44e-118	1	367	2	372	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	5.90e-87	2	367	18	376	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	3.36e-57	22	367	23	373	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	3.41e-20	46	361	1	312	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
QBE96063.1	1.79e-181	1	367	1	367
QIB56106.1	3.61e-181	1	367	1	367
QMW81160.1	3.61e-181	1	367	1	367
ASU30578.1	2.80e-178	1	367	1	367
QQQ95376.1	2.80e-178	1	367	1	367

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	9.05e-71	1	365	5	383	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	2.16e-56	2	361	20	389	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]
6FV3_A	1.77e-51	47	367	64	386	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	2.63e-50	47	367	64	386	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]
1O12_A	1.26e-47	19	367	31	366	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34450	4.96e-70	1	365	5	383	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
A7MBC0	1.13e-60	2	361	20	389	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q6P0U0	3.52e-57	18	361	29	389	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
P34480	9.73e-57	5	361	25	401	N-acetylglucosamine-6-phosphate deacetylase OS=Caenorhabditis elegans OX=6239 GN=F59B2.3 PE=3 SV=1
P96166	2.39e-56	3	363	15	375	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD 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
1.000046	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000035_01637.