CAZyme Information: MGYG000000179_04279

Basic Information

• Species: Enterocloster aldenensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster aldenensis
• CAZyme ID: MGYG000000179_04279
• CAZy Family: CE9
• CAZyme Description: N-acetylgalactosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
394	MGYG000000179_14|CGC1	43010.12	5.7883

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000179	6044848	Isolate	China	Asia

• Gene Location: Start: 99073; End: 100257 Strand: +

Full Sequence      

MEHFIFTNARIVLPDTILDDHYLSVKNGVIESIGKGTPDREQLNSCTTVDCGGQYLSPGF
IDIHCHGGGGADFMDGHMEDILTAARAHLIHGTTGICPTTLTCSDEELFTFFESFRQARE
VTEQMPHLLGIHLEGPYFSPAQAGAQPPKYLVHPRPEHYHEILRRGQGNIVRWSAAPELP
GALELGDELAGKGIKVSMGHSDAGFEDIVNAMEHGYSQITHFYSAMSTITRKRGRRVLGL
IECGYLFDRLKVEIIADGIHLPPELLKLILKCKNHDDICLVTDSMRGAGMPDGPSLLGSK
KNGVPVIIEDGIANMPDFSSFAGSVATTDRLVRVMVQKAGLPVWEAVKMASLNPASFLGI
QETYGSIQPGKSADLLIFDDDIRISSVYVSGIRQ

Enzyme Prediction     

No EC number prediction in MGYG000000179_04279.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	6	391	2.1e-116	0.9973190348525469

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	4.97e-142	5	391	2	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	1.14e-120	5	391	3	375	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	4.50e-80	2	391	3	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	3.97e-59	6	391	4	376	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	4.61e-25	55	390	1	320	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
AEV28731.1	2.70e-153	6	391	4	387
QTQ14483.1	5.64e-149	5	391	2	404
QTQ16716.1	1.61e-148	5	391	2	404
QTQ11346.1	9.21e-148	5	391	2	404
ADY12033.1	4.05e-134	5	393	3	392

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FV3_A	7.12e-51	2	391	15	389	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	1.05e-49	2	391	15	389	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]
2VHL_A	1.17e-43	2	384	3	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	1.53e-43	6	391	15	398	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	4.27e-41	56	391	53	369	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
Q5BJY6	1.79e-49	6	391	15	398	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
Q8JZV7	2.51e-49	6	391	15	398	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
Q8XAC3	9.04e-49	10	391	9	372	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
P96166	6.46e-45	26	391	31	382	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q6P0U0	7.18e-45	6	391	15	398	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 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
1.000065	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000179_04279.