CAZyme Information: POW20237.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW20237.1
• CAZy Family: GH81
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
482		54076.22	8.4994

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=PKSM01000036:185477-190969(-)

Full Sequence      

MNTILRLSFVVAFFLLSFIQSRSLKKAAIVKYAPPATTCSRPGLVSLTFDDGPFDFETEI
SDYLHARKIQSTFFVNGNNWGCIYDESIVQQLKHTWSHANISTLSAERLHQELDLIEEAL
IKIIGAKPKFFRPPYGSYDQKSLGILKERGYVVANWTFDSGDAVGATPEQSIGGYRNLAK
KFPSSQITLNHETYQTTAEKVIPYAVPLLQKAGYRLVHMSECLGTGTNINDLYQWIGKPS
ERDFVRSDPATTCSRPRLAALTFDDGPYNYENRISDYLHARQIKGTFFVNGNNYGCIYDE
STVQRLKRSFYQGHLIASHTWSHANISTLSATQLHRQLDLVERALMKILGVKPKFFRAPY
GEHNQQSLDILKKRGYIVIDWSFDSGDSIGATLEESMKAYNQLAKKFPASQIALNHETYQ
ATAEKVTPYAVSMLQKAGYKLVHVSECLGTGTNINDLYQFVGKPSARDSSWTCSGTPASE
GN

Enzyme Prediction     

EC	3.5.1.41:1	3.1.1.72:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	255	377	1.1e-27	0.8923076923076924
CE4	42	155	3.6e-22	0.9076923076923077

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	1.19e-78	251	444	2	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.
200575	CE4_ClCDA_like	2.48e-68	37	217	2	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	2.55e-41	257	426	1	163	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.
213022	CE4_NodB_like_6s_7s	3.18e-37	43	210	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.
200569	CE4_SmPgdA_like	9.86e-34	261	440	5	186	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAJ90973.1|CE4	1.38e-128	248	482	35	269
ALL40836.1|CE4	3.73e-77	252	473	57	274
QRV78597.1|CE4	2.22e-71	236	474	18	249
QRW07526.1|CE4	2.45e-70	236	474	18	249
QRV93375.1|CE4	3.45e-70	236	474	18	249

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IW0_A	3.70e-33	249	449	34	239	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
7BLY_A	6.41e-26	240	449	23	228	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
5LFZ_A	1.58e-25	245	453	13	208	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
5O6Y_A	4.15e-21	260	418	24	175	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]
5O6Y_B	5.01e-20	260	418	24	175	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_D Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6DWK3|CDA_COLLN	8.55e-33	249	449	34	239	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|A0A1L3THR9|CDA_PESTX	7.33e-32	251	449	33	229	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4AM78|CDA_ARTBC	7.44e-27	253	449	164	360	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|D4B5F9|PGDA_ARTBC	1.52e-25	252	449	144	341	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|Q81EK9|PGDA1_BACCR	7.15e-20	260	418	84	235	Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_1960 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.004161	0.995792	CS pos: 21-22. Pr: 0.9418

TMHMM  Annotations     

There is no transmembrane helices in POW20237.1.