dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003910_00589

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Dysosmobacter;

CAZyme ID

MGYG000003910_00589

CAZy Family

CE9

CAZyme Description

Adenine deaminase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410	MGYG000003910_18\|CGC1	43881.52	6.555

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003910	2471901	MAG	China	Asia

Gene Location

Start: 11701; End: 12933 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003910_00589.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	40	405	4.9e-123	0.9865951742627346

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00854	NagA	1.17e-129	34	405	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	1.11e-119	36	405	4	375	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
TIGR00221	nagA	2.55e-85	52	405	33	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
PRK11170	nagA	8.25e-56	71	386	45	358	N-acetylglucosamine-6-phosphate deacetylase; Provisional
pfam01979	Amidohydro_1	3.40e-18	76	408	1	325	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIA31363.1	2.95e-127	34	410	1	373
ANU41013.1	2.95e-127	34	410	1	373
QQR06201.1	2.95e-127	34	410	1	373
AEN97408.1	1.60e-102	34	408	1	380
ARD64548.1	1.03e-100	34	408	1	370

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FV3_A	5.08e-58	77	405	64	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	7.61e-57	77	405	64	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]
7NUT_A	5.32e-55	8	408	3	401	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]
2VHL_A	2.95e-54	77	405	55	384	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]
3EGJ_A	6.17e-45	36	405	7	376	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
Q8XAC3	2.19e-61	30	392	6	360	N-acetylgalactosamine-6-phosphate deacetylase OS=Escherichia coli O157:H7 OX=83334 GN=agaA PE=1 SV=2
A7MBC0	2.75e-60	34	408	31	401	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
Q8JZV7	3.17e-58	34	408	31	401	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
Q5BJY6	2.41e-57	34	408	31	401	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
Q9Y303	2.91e-54	8	408	3	401	N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2

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
1.000030	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003910_00589.