CAZyme Information: VDB89247.1

Basic Information

• Species: Blumeria graminis
• Lineage: Ascomycota; Leotiomycetes; ; Erysiphaceae; Blumeria; Blumeria graminis
• CAZyme ID: VDB89247.1
• CAZy Family: GH93
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
778	LR026990|CGC4	85601.42	5.1040

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BgraminisTritici96224	8470	1268274	123	8347

• Gene Location: location=LR026990:7937839-7940287(-)

Full Sequence      

MNLLILQLLFIIWPRVALSNCTSDIAIDAYQDRVSKKNNWHLYTFDDGTTSGFTRVLSKK
KVFFEATSARSYVFTEFPCQNLTGTSYDALTFSLRGPEDASYVLELQTSASCSTKEYASN
FVSLTGVTSVAQTFTIPLSLFEGANLEAIKSIVFQDLTLGDWEIGETELSCTETTAHSIS
SDARNSSNTINSLSSTTTQQTLKRQNPEPCESLLIDDFASQSRLTFLFYNAKLFPSSDDA
TMKPVAGRVDTQTSVIVADNHVTLTPANDKSYWFTQLGCLKATNTWGGIGMTIKAARGTT
LRLEIGSDPSCTNTNPKNVAVSSTQLGWNFDGTEKYYQIPFSKFPGLDTDHLVTLLFSEM
SKSVTLGPIALYCGTSGSAYTIPMMTEPVESDEKIPTTRGQSMLLIDTFMNKDSNSLGFY
HGGDDSQVATIANSRLTINTKGNADLSWYTQVANGCRDLTPLQDGYLHIAYSGSNAFTVA
LQQHNPTCNDKIRPIPFTWDSVEASRYSNSVKSDIYVPLTHFNIDRTKSIGFGFQGFYTS
NPTTFSKIEIVSSVPSGFLVPSKLPTASLVFSCTRPNSFAFAIDDGEPKFAQRIVSAVAE
AGIKVTFFTVGAPLLDPSTNLTNVYKGMLDSGHQVAYHSYTHPPMEGLPSLAAIDWELNN
DIDAVKKTLGITSTYFRPPFGTEGARVRQRLESIIPGSKFVMWSVDVQDYLWAQSPTPEN
QITNFENDVKLGGNLVVMHYLYETTVNYLPKFIAIAKSTGKQLMRVDQCMEDPNAPPL

Enzyme Prediction     

No EC number prediction in VDB89247.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	574	689	1.2e-16	0.8384615384615385

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	3.00e-37	577	757	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	9.11e-36	570	766	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.
200578	CE4_CtAXE_like	3.61e-24	580	768	4	179	Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.
200584	CE4_GT2-like	2.82e-23	584	766	8	191	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.
200571	CE4_SpPgdA_BsYjeA_like	8.02e-23	580	766	4	177	Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs. This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCT74190.1|CE4	1.34e-22	570	773	34	234
QGI86985.1|CE4	1.34e-22	570	773	34	234
QGJ00522.1|CE4	1.34e-22	570	773	34	234
QGI69634.1|CE4	1.34e-22	570	773	34	234
QKD61170.1|CE4	1.81e-22	570	773	34	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2CC0_A	2.54e-12	584	760	12	176	Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans],2CC0_B Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L3THR9|CDA_PESTX	6.71e-18	562	775	24	233	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4B5F9|PGDA_ARTBC	4.01e-13	564	775	136	345	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|J9VPD7|CDA1_CRYNH	4.64e-13	570	752	152	318	Chitin deacetylase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA1 PE=1 SV=1
sp|A0A0H3GDH9|PGDA_LISM4	1.33e-11	549	768	240	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain 10403S) OX=393133 GN=pgdA PE=2 SV=1
sp|A0A3Q0NBH7|PGDA_LISMG	1.33e-11	549	768	240	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) OX=1334565 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000217	0.999746	CS pos: 19-20. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in VDB89247.1.