CAZyme Information: POW22481.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW22481.1
• CAZy Family: GT39
• CAZyme Description: Chitin deacetylase [Source:UniProtKB/TrEMBL;Acc:A0A2S4WL56]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
596	PKSM01000009|CGC1	66559.69	7.1307

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2	14629	N/A	0	14629

• Gene Location: location=PKSM01000009:307747-312317(-)

Full Sequence      

MGFTRLLTLVVTVASLLRFDQVIAAHTNSSLRVRQNTAVPVYNTCTVPRSFALTFDMGLY
GYSEKLDEQMPKEASLSMGKTGDAFMTPPTNCLQDSTRGILSGAILGSHVHLNQGTYDQI
DVTRIAGTAMIKILGVKPLYMRPPYGEYNDVVKRVFLRKALSPSHKTQLQVLRNRGYKGL
VMWSQDSGDTHIPAPSSSPVIRSYRSYPEKTIVLNHEVKDFTVEEVIPAVIPILQRKGFS
LQTVPECLGLSSDPADWYVRVQEAGTRDDSWTARVLRYPASSNRKVTCLSLKDFEAICLL
HCSSSFISTKRNKSLGFQSQEGMGFTRLLTLVVTVASLLRFDQVTGAHTNDIRTLRARQD
TAVPVYDTCTVPGSFALTFDDGPYGFSTRLDSTLNAANAKGSFFINGQNWGCIYDYADVL
LERFNNGHFIASHTWSHVHMNQGTYEQLSHQLELVEQAMIRILGVKPLYMRPPYGEYNDV
VLQVLRDRGYKGLIMWNQDSGDTFTPTPSSAQIIDSYRSFPEKTISLNHEIKDFTVDQVI
PAVIPILQQKGFSLQTVPEALGLSSDPADWYVRVQEPGTRDDSWTCEATPLPGNFE

Enzyme Prediction     

EC	3.5.1.41:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	372	491	9.2e-23	0.8846153846153846

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	7.33e-79	366	557	1	197	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	1.53e-40	373	548	1	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.
200575	CE4_ClCDA_like	8.98e-36	42	244	1	197	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.
200569	CE4_SmPgdA_like	1.18e-32	377	556	5	189	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.
396211	Polysacc_deac_1	3.87e-32	369	491	3	122	Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALL40879.1|CE4	4.26e-74	355	586	25	253
ALL40640.1|CE4	3.84e-70	358	552	39	233
CAJ90973.1|CE4	6.83e-59	368	592	39	266
QRV93375.1|CE4	7.62e-58	365	586	31	248
ALL40836.1|CE4	2.27e-57	362	586	51	274

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Y8U_A	8.89e-25	365	562	25	222	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
7BLY_A	2.76e-24	365	571	32	235	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2IW0_A	6.05e-23	369	571	38	246	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
5LFZ_A	2.27e-21	359	571	11	215	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
7FBW_A	6.51e-20	376	561	120	300	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L3THR9|CDA_PESTX	3.01e-34	359	571	22	236	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4AM78|CDA_ARTBC	1.33e-30	365	571	160	367	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|D4B5F9|PGDA_ARTBC	2.06e-30	361	571	134	348	Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
sp|Q5AQQ0|CDA_EMENI	5.37e-24	365	562	32	229	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	1.49e-22	369	571	38	246	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000233	0.999759	CS pos: 24-25. Pr: 0.9802

TMHMM  Annotations     

There is no transmembrane helices in POW22481.1.