dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: PMAA_086850-t26_1-p1

You are here: Home > Sequence: PMAA_086850-t26_1-p1

Basic Information help

Species

Talaromyces marneffei

Lineage

Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei

CAZyme ID

PMAA_086850-t26_1-p1

CAZy Family

GH92

CAZyme Description

N-acetylglucosamine-6-phosphate deacetylase (NagA), putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
475	DS995901\|CGC15	51461.29	5.9347

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in PMAA_086850-t26_1-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	217	449	2.5e-76	0.6193029490616622
CE9	15	178	1.9e-36	0.4101876675603217

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238434	NagA	3.68e-128	13	466	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.
224733	NagA	7.65e-99	13	471	2	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
272968	nagA	1.95e-74	56	445	45	366	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
183010	nagA	2.92e-59	51	444	36	362	N-acetylglucosamine-6-phosphate deacetylase; Provisional
396526	Amidohydro_1	9.79e-15	64	469	1	335	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
0.0	1	475	1	475
4.16e-273	1	474	1	448
3.10e-219	1	474	1	423
3.10e-219	1	474	1	423
3.10e-219	1	474	1	423

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.74e-85	11	449	11	389	Chain A, 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]
6.68e-48	15	444	7	362	N-acetylglucosamine-6-phosphate deacetylase 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]
1.85e-41	64	445	54	371	The Three-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]
1.95e-34	56	464	59	393	Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_B Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_C Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida],6JKU_D Crystal structure of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella Multocida [Pasteurella multocida]
2.63e-34	26	450	14	361	Crystal structure 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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.40e-87	1	464	1	403	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
2.16e-86	11	447	25	398	N-acetylglucosamine-6-phosphate deacetylase OS=Drosophila melanogaster OX=7227 GN=CG17065 PE=2 SV=1
2.95e-84	11	449	11	389	N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
9.14e-83	12	474	12	406	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
1.29e-82	12	449	12	389	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000000

TMHMM Annotations help

There is no transmembrane helices in PMAA_086850-t26_1-p1.