CAZyme Information: HVAS_10127230.1-p1

Basic Information

• Species: Hemileia vastatrix
• Lineage: Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix
• CAZyme ID: HVAS_10127230.1-p1
• CAZy Family: GH27
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
168		19528.30	7.5867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HvastatrixRaceXXXIII	12854	N/A	284	12570

• Gene Location: location=PHNK01012723:9549-10352(+)

Full Sequence      

FDDGINQYGPELDQTLNRYHTRATFFINGNNWDCIYNHADVLVTRFNQGHLLANHGWSHT
HMDQLTADQMHHQLWLVEKAMIEILGVKPRIFRPPYVLAQRGYVALLMWSQDSGDTFTPT
PSPNQIVEKYKTFPARTIVLNHEVKDFTVKQVIPQVIPLLQKKSYNLV

Enzyme Prediction     

EC	3.5.1.41:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	1	97	8.4e-19	0.7153846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	8.90e-55	1	168	14	195	Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine), to carry out acid/base catalysis. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA.
213022	CE4_NodB_like_6s_7s	3.53e-33	1	161	7	171	Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.
200574	CE4_BsYlxY_like	1.67e-28	6	168	18	182	Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.
200569	CE4_SmPgdA_like	9.50e-27	1	165	7	185	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
200584	CE4_GT2-like	1.88e-26	1	168	7	189	Catalytic NodB homology domain of uncharacterized bacterial glycosyl transferase, group 2-like family proteins. This family includes many uncharacterized bacterial proteins containing an N-terminal GH18 (glycosyl hydrolase, family 18) domain, a middle NodB-like homology domain, and a C-terminal GT2-like (glycosyl transferase group 2) domain. Although their biological function is unknown, members in this family contain a middle NodB homology domain that is similar to the catalytic domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily. The presence of three domains suggests that members of this family may be multifunctional.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALL40640.1|CE4	3.84e-61	1	168	60	236
ALL40879.1|CE4	8.68e-50	2	163	48	218
CAJ90973.1|CE4	1.58e-42	1	168	50	229
CCA65368.1|CE4	3.06e-40	48	144	18	123
QRV93375.1|CE4	4.15e-35	1	168	45	222

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LFZ_A	4.84e-19	1	168	31	198	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2C1G_A	1.16e-16	1	168	242	410	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2C1I_A	5.52e-16	1	168	242	410	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
2IW0_A	3.04e-13	1	168	48	232	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
2Y8U_A	2.26e-12	1	97	39	132	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8DP63|PGDA_STRR6	6.36e-16	1	168	274	442	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
sp|A0A1L3THR9|CDA_PESTX	7.34e-16	1	96	45	140	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	7.64e-13	1	168	48	232	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|Q55U20|CDA2_CRYNB	2.64e-12	1	148	164	328	Chitin deacetylase 2 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA2 PE=1 SV=1
sp|Q5AQQ0|CDA_EMENI	1.26e-11	1	97	46	139	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000074	0.000001

TMHMM  Annotations     

There is no transmembrane helices in HVAS_10127230.1-p1.