dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: CAX41378.1

You are here: Home > Sequence: CAX41378.1

Basic Information help

Species

Candida dubliniensis

Lineage

Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida dubliniensis

CAZyme ID

CAX41378.1

CAZy Family

GH2

CAZyme Description

NAG2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
413	FM992693\|CGC6	45342.89	6.1246

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CdubliniensisCD36	6095	573826	235	5860

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.5.1.25:5

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE9	6	390	4.8e-109	0.9919571045576407

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238434	NagA	1.31e-140	4	392	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	1.38e-91	44	395	41	378	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
272968	nagA	5.46e-59	35	381	36	368	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
183010	nagA	9.66e-48	6	398	4	382	N-acetylglucosamine-6-phosphate deacetylase; Provisional
396526	Amidohydro_1	3.09e-07	52	395	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
1.17e-309	1	413	1	413
6.87e-293	1	413	1	413
6.87e-293	1	413	1	413
6.87e-293	1	413	1	413
6.87e-293	1	413	1	413

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.35e-74	5	399	14	405	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]
7.05e-45	7	397	8	381	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]
7.81e-37	18	395	13	379	Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YMY_B Crystal Structure of the N-Acetylglucosamine-6-phosphate deacetylase from Escherichia coli K12 [Escherichia coli K-12],1YRR_A Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],1YRR_B Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution [Escherichia coli],2P50_A Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_B Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_C Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12],2P50_D Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn [Escherichia coli K-12]
4.00e-36	18	395	13	379	Chain A, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12],2P53_B Chain B, N-acetylglucosamine-6-phosphate deacetylase [Escherichia coli K-12]
1.28e-33	52	379	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.91e-75	4	395	13	401	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
4.96e-74	5	399	14	405	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1
1.95e-73	5	399	14	405	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
2.75e-73	5	399	14	405	N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
1.95e-72	46	395	64	413	N-acetylglucosamine-6-phosphate deacetylase OS=Caenorhabditis elegans OX=6239 GN=F59B2.3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000026	0.000009

TMHMM Annotations help

There is no transmembrane helices in CAX41378.1.