CAZyme Information: MGYG000001502_00323

Basic Information

• Species: Intestinimonas massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Intestinimonas; Intestinimonas massiliensis
• CAZyme ID: MGYG000001502_00323
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382		40130.73	5.1901

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001502	3103033	Isolate	not provided	not provided

• Gene Location: Start: 274250; End: 275398 Strand: +

Full Sequence      

MIIKNGTLFCEGGSFRTMDLKIQNGHIAEIGSQLAADGQESLDATNCYVVPGLVDIHIHG
AVGADFSDGEGASIQTMARFLLSQGVTSFLGTSMALPGERLSQIYRTARPFVGQAVPGMA
TLRGVNMEGPFFNVEKRGAQNPDFIIPPNLDLFLRLQEDSGGAIRTVAVAPETEGGLEFV
EKASRMCSVSLAHSCADYETSRQAFARGANHVTHVFNGMPAFHHRDPGIVGAAVGTDAYV
ELICDGVHVHPAVVQSVFRLFGEDRVCLISDAMRACGMPDGEYDLGGQAVTVANGCATIA
TGSLAGSITVLTDCLRRAVGFGIPLEAALKAATINPARSVGLDREIGSLACGKQADILVL
DRALSLRNIVLNGELQAVSGLS

Enzyme Prediction     

No EC number prediction in MGYG000001502_00323.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	3	373	2.2e-124	0.9973190348525469

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	1.87e-144	1	373	1	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	2.06e-130	1	375	2	377	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
PRK11170	nagA	3.34e-52	51	374	53	377	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	7.08e-22	48	361	1	309	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.
COG1228	HutI	3.41e-14	1	361	12	374	Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADZ84961.1	9.13e-118	1	373	1	375
QEH70419.1	9.13e-118	1	373	1	375
QCP34781.1	4.52e-114	1	375	1	369
QNO15303.1	4.82e-114	2	374	4	372
QIA31363.1	2.58e-113	35	375	31	370

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHL_A	6.98e-64	1	379	5	390	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	1.10e-52	11	375	22	400	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	2.59e-47	51	374	55	370	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]
6FV3_A	6.57e-46	20	374	36	390	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	9.49e-45	20	374	36	390	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	3.76e-68	1	376	6	382	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O34450	3.82e-63	1	379	5	390	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P96166	2.07e-59	23	375	31	384	N-acetylglucosamine-6-phosphate deacetylase OS=Vibrio furnissii OX=29494 GN=manD PE=3 SV=1
Q8XAC3	1.39e-57	2	375	4	374	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
A7MBC0	1.57e-57	11	375	22	400	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
1.000053	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001502_00323.