CAZyme Information: PUG3_T012387-RA-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PUG3_T012387-RA-p1
• CAZy Family: GT22
• CAZyme Description: Amidohydrolase domain containing 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
232		25136.42	6.6867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumBR650	14086	1223559	0	14086

• Gene Location: location=PultBR650_SC2199:1048-1965(+)

Full Sequence      

MLGLHLEGPFVSAERKGAHNESVLLAPVDGIASLEQRYGALDNVAXXXXRIGRRDGHDSG
SERKGDRYQRGHVFNAMGPFHHRDPGLIGLLGLTHNRPYYGLILDGLHSHRTSARIIRSC
HPEGLASGEYVLAGKRVDVKKNGAFLVDTDTIAGSIVTMDSCVRTLIEYTGCSIEEALVA
ASTRPAQVLGIANRKGTLEFGADADFVLLNDDLHVLHTYIAGELVFDASTLH

Enzyme Prediction     

EC	3.5.1.25:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE9	72	222	6.4e-45	0.4316353887399464

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238434	NagA	2.40e-66	1	222	120	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	2.11e-56	2	227	122	380	N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].
272968	nagA	2.34e-43	1	222	125	379	N-acetylglucosamine-6-phosphate deacetylase. [Central intermediary metabolism, Amino sugars]
183010	nagA	1.58e-24	2	227	126	381	N-acetylglucosamine-6-phosphate deacetylase; Provisional
238634	Met_dep_hydrolase_C	2.75e-10	171	226	299	359	Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAI60548.1|CE9	5.02e-56	1	229	137	405
CBG19248.1|CE9	7.07e-55	1	225	137	401
AAH65449.1|CE9	7.07e-55	1	225	137	401
ARA90557.1|CE9	2.59e-54	1	231	129	398
AAI51479.1|CE9	4.40e-54	1	225	137	401

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7NUT_A	3.01e-55	1	228	137	404	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]
2VHL_A	1.76e-30	1	226	130	388	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]
1O12_A	2.92e-21	1	226	121	373	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]
2P53_A	1.92e-19	2	225	126	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]
1YMY_A	3.61e-19	2	225	126	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6P0U0|NAGA_DANRE	1.26e-55	1	225	137	401	N-acetylglucosamine-6-phosphate deacetylase OS=Danio rerio OX=7955 GN=amdhd2 PE=2 SV=1
sp|A7MBC0|NAGA_BOVIN	7.81e-55	1	225	137	401	N-acetylglucosamine-6-phosphate deacetylase OS=Bos taurus OX=9913 GN=AMDHD2 PE=2 SV=1
sp|Q9Y303|NAGA_HUMAN	1.55e-54	1	228	137	404	N-acetylglucosamine-6-phosphate deacetylase OS=Homo sapiens OX=9606 GN=AMDHD2 PE=1 SV=2
sp|Q5BJY6|NAGA_RAT	1.69e-53	1	228	137	404	N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2
sp|Q8JZV7|NAGA_MOUSE	2.38e-53	1	228	137	404	N-acetylglucosamine-6-phosphate deacetylase OS=Mus musculus OX=10090 GN=Amdhd2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999982	0.000037

TMHMM  Annotations     

There is no transmembrane helices in PUG3_T012387-RA-p1.