CAZyme Information: MGYG000001562_00490

Basic Information

• Species: Alistipes timonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes timonensis
• CAZyme ID: MGYG000001562_00490
• CAZy Family: CE9
• CAZyme Description: N-acetylglucosamine-6-phosphate deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
416	MGYG000001562_11|CGC7	44046.48	6.1275

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001562	3488594	Isolate	not provided	not provided

• Gene Location: Start: 368432; End: 369682 Strand: +

Full Sequence      

MKTLLPIFGALACCLPAAAETTHRVKIINAAVVMPSKVVENATILIENGRIAAVGTDLGE
AFEGAEIIDAAGRYAAPGFIDVHCHGGGGHDFSDGTVEAMLGAAEMHAQHGTTLIYPTTA
SCSNATLFSLFDTYRKAVKKNTRGAAFGGIHIEGGYLSMEMKGGQDPRYIKNPTPEDYNA
ILAKGGDLIARWTFAPELPGSDALIGELARRGIQMSMGHTSALYDEAVSAYDAGMSSITH
FYSMCSGVTRRNALRYAGVIEAGYLLDGLYVETIGDGIHLPEPLLRLIWKVKGPDRIVGI
TDAMRGAGMPDGPTVLGSIDDGVPAIIEDGVAKLPDRSSFAGSVCTTDRVVRSYVTKTGA
SLPEAVQVVTLSPARLMHIDDRKGSVTPGKDADIVLFDKDINITLTMIGGKVVYRK

Enzyme Prediction     

No EC number prediction in MGYG000001562_00490.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	28	410	8.2e-108	0.9946380697050938

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	1.63e-134	26	410	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	1.20e-109	27	415	4	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	6.17e-79	27	411	7	380	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	3.04e-51	27	413	4	379	N-acetylglucosamine-6-phosphate deacetylase; Provisional
COG1228	HutI	2.51e-23	35	416	22	403	Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI64809.1	1.14e-151	24	416	3	393
QRX64347.1	2.15e-149	23	415	3	395
SCD19170.1	3.50e-148	23	415	3	395
AYQ35214.1	4.82e-147	24	416	2	391
AXE19558.1	2.86e-146	24	416	2	391

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FV3_A	1.03e-46	46	411	38	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]
1O12_A	2.25e-46	77	415	55	374	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]
6FV4_A	1.48e-45	46	411	38	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]
2VHL_A	1.90e-44	31	414	11	388	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	2.53e-38	69	415	57	403	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q84F86	1.17e-44	29	412	10	381	N-acetylglucosamine-6-phosphate deacetylase OS=Lysinibacillus sphaericus OX=1421 GN=nagA PE=2 SV=1
O34450	1.04e-43	31	414	11	388	N-acetylglucosamine-6-phosphate deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagA PE=1 SV=1
P44537	4.14e-41	24	411	2	377	N-acetylglucosamine-6-phosphate deacetylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagA PE=3 SV=1
Q6P0U0	2.47e-40	68	416	56	404	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
Q5BJY6	5.26e-40	69	415	57	403	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000582	0.649852	0.348809	0.000272	0.000255	0.000220

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001562_00490.